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Information on EC 4.2.1.1 - carbonic anhydrase
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4.2.1.1 carbonic anhydraseIUBMB Comments
The enzyme catalyses the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. Three distinct classes exist, and appear to have evolved independently. Contains zinc.
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-
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-
beta-blockers
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cystoid
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thiazide
- medicine
- hydrochlorothiazide
- analysis
-
glaucomatous
The enzyme appears in viruses and cellular organisms
Synonyms
carbonic anhydrase, ca ix, ca ii, hca ii, hca i, carbonic anhydrase ix, carbonic anhydrase ii, hca ix, ca iv, anhydrase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkalistable alpha-carbonic anhydrase
alpha carbonic anhydrase
alpha-CA
alpha-carbonic anhydrase
alpha-class carbonic anhydrase
alpha-type CA
alpha-type carbonic anhydrase
anhydrase
-
-
-
-
bCA IV
beta-CA
beta-carbonic anhydrase
beta-class carbonic anhydrase
BhCA
bsCA I
bsCA II
CA
CA 1
CA 3
CA I
CA II
CA III
CA IV
CA IX
CA VA
CA VB
CA VI
CA VII
CA XII
CA XIII
CA XIV
Ca XV
CA-I
CA-II
CA-IX
-
-
-
-
CA-VA
-
-
-
-
CA-VB
-
-
-
-
CA-VI
CA-VII
-
-
-
-
CA-XII
-
-
-
-
CA-XIV
-
-
-
-
CA1
CA2
CA3
CA9
CAA1
CAA2
Cab
CAH3
CAH7
CAH8
CAI
CAII
CAIII
CAIV
CAIX
Cam
CamH
carbonate anhydrase
-
-
-
-
Carbonate dehydratase
-
-
-
-
Carbonate dehydratase IX
-
-
-
-
Carbonate dehydratase VA
-
-
-
-
Carbonate dehydratase VB
-
-
-
-
Carbonate dehydratase VI
Carbonate dehydratase VII
-
-
-
-
Carbonate dehydratase XII
-
-
-
-
Carbonate dehydratase XIV
-
-
-
-
carbonate hydro-lyase
carbonate hydrolyase
carbonic acid anhydrase
-
-
-
-
carbonic anhydrase
carbonic anhydrase 1
carbonic anhydrase 2
carbonic anhydrase 3
carbonic anhydrase cambialistic enzyme
carbonic anhydrase I
carbonic anhydrase II
carbonic anhydrase III
carbonic anhydrase isozyme IV
carbonic anhydrase IV
carbonic anhydrase IX
carbonic anhydrase V
carbonic anhydrase VI
carbonic anhydrase XII
carbonic anhydrase XIII
carbonic anhydrase XIV
carbonic anhydrase XV
carbonic anhydrase-I
carbonic dehydratase
-
-
-
-
carboxyanhydrase
-
-
-
-
CcmM
CDCA1
CmCA
CpsCA
CpsCAgamma
cynT
dehydratase, carbonate
-
-
-
-
DVU_1777
eCA
extracellular carbonic anhydrase
gamma-CA
gamma-carbonic anhydrase
gamma-class carbonic anhydrase
HCA
hCA I
HCA II
hCA III
hCA IV
hCA IX
hCA XII
hCAII
HICA
human carbonic anhydrase II
human carbonic anhydrase III
Ice-CA
Membrane antigen MN
-
-
-
-
Nce103
NstCcmM209
P54/58N
-
-
-
-
PERMA_1443
PgiCAb
PGJ_00014320
PMCA
pMW1
-
-
-
-
RCC-associated antigen G250
-
-
-
-
Renal cell carcinoma-associated antigen G250
-
-
-
-
Rv1284
Rv3273
Salivary carbonic anhydrase
SazCA
Secreted carbonic anhydrase
SspCA
SULAZ_0541
TacA
Tcru
Tcr_1545
Theam_1576
Tumor antigen HOM-RCC-3.1.3
-
-
-
-
TweCA
additional information
alkalistable alpha-carbonic anhydrase
Halalkalibacterium halodurans TSLV1 / MTCC 10961
-
-
beta-CA
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
-
CA
-
-
-
-
CA II
-
-
CA-VI
-
-
-
-
CA1
-
-
-
-
CA2
-
-
-
-
Cab
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
-
CAIX
-
-
-
-
Carbonate dehydratase VI
-
-
-
-
carbonic anhydrase
-
-
-
-
carbonic anhydrase
-
-
carbonic anhydrase
-
-
carbonic anhydrase
-
carbonic anhydrase II
-
-
carbonic anhydrase II
-
carbonic anhydrase III
-
the enzyme possesses only low carbon dioxide hydratase activity
hCA I
-
HCA II
-
hCA IX
-
Salivary carbonic anhydrase
-
-
-
-
Secreted carbonic anhydrase
-
-
-
-
additional information
HICA is a type II member of the beta-carbonic anhydrase family
additional information
-
the enzyme from Methanosorcina thermophila belongs to the gamma class carbonic anhydrases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
H2CO3 = CO2 + H2O
carbonic anhydrase III is limited in rate by a step occuring outside the actual interconversion of CO2 and HCO3- and involving a change in bonding to hydrogen exchangeable with solvent water
-
H2CO3 = CO2 + H2O
zinc-hydroxide mechanism, rate-determining H+ transfer step in catalytic mechanism
-
H2CO3 = CO2 + H2O
reaction mechanism, model of the active site designed on the basis of the X-ray crystal structure, proposed for both metal ions similar reaction pathways consisting in the nucleophilic attack by the metal bound hydroxide to the carbon dioxide with bicarbonate formation, in a next internal rotation of this last fragment, and then in the formation of a species ready for the product removal, overview
-
H2CO3 = CO2 + H2O
reaction mechanism, model of the active site designed on the basis of the X-ray crystal structure, proposed for both metal ions similar reaction pathways consisting in the nucleophilic attack by the metal bound hydroxide to the carbon dioxide with bicarbonate formation, in a next internal rotation of this last fragment, and then in the formation of a species ready for the product removal, overview
-
H2CO3 = CO2 + H2O
the rate limiting step in catalysis of bicarbonate dehydration by HCA II is an intramolecular proton transfer from His64 to the zinc-bound hydroxide
-
H2CO3 = CO2 + H2O
interconversion of CO2 and water to bicarbonate and a proton. The general catalysis of CA is a metal-hydroxide ping-pong mechanism composed of two independent steps. The first step of catalysis is initiated by nucleophilic attack on the carbon of CO2 by the metal-bound hydroxide to yield bicarbonate, which is subsequently displaced by a water molecule. The second step is the removal of a proton from the now metal-bound water via an ordered water network and a residue acting as a weak base, which is typically a His at the opening of the active site
H2CO3 = CO2 + H2O
reaction mechanism, analysis of the restoring step of the carbonic anhydrase catalytic cycle for natural and promiscuous substrates, natural HCO3-x02and promiscuous H2NCOHN- products, catalytic reaction mechanism, NPT molecular dynamics simulations, overview
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
-
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
-
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
-
-
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
Desulfovibrio vulgaris Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303
-
-
H2CO3 = CO2 + H2O
interconversion of CO2 and water to bicarbonate and a proton. The general catalysis of CA is a metal-hydroxide ping-pong mechanism composed of two independent steps. The first step of catalysis is initiated by nucleophilic attack on the carbon of CO2 by the metal-bound hydroxide to yield bicarbonate, which is subsequently displaced by a water molecule. The second step is the removal of a proton from the now metal-bound water via an ordered water network and a residue acting as a weak base, which is typically a His at the opening of the active site
-
-
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
Persephonella marina DSM 14350 / EX-H1
-
-
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
-
H2CO3 = CO2 + H2O
the catalytic mechanism for the CO2 hydration reaction consists of two steps. In the first step a zinc-bound hydroxide leads the nucleophilic attack on a CO2 molecule with formation of bicarbonate bound to the zinc ion, which is then substituted by a water molecule. The second step, the rate limiting one, consists of the regeneration of the enzyme reactive species, the zinc-bound hydroxide, via a proton transfer reaction, which occurs from the zinc-bound water molecule to the external buffer. This process is generally assisted by an enzyme residue which acts as proton shuttle
Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1
-
-
H2CO3 = CO2 + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
-
-
-
-
dehydration
elimination
-
-
-
-
hydration
dehydration
-
-
dehydration
-
-
hydration
-
-
hydration
-
-
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SYSTEMATIC NAME
IUBMB Comments
carbonic acid hydro-lyase (carbon-dioxide-forming)
The enzyme catalyses the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. Three distinct classes exist, and appear to have evolved independently. Contains zinc.
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CAS REGISTRY NUMBER
COMMENTARY
9001-03-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
CO2 + H2O
H2CO3
-
periplasmic alpha-carbonic anhydrase activity of Helicobacter pylori is essential for acid acclimation
-
-
?
CO2 + H2O
H2CO3
-
-
696613, 696737, 696955, 697525, 699227, 699426, 699957, 700140, 700410, 700971, 701131, 702470, 702518, 702571, 702654
-
-
r
CO2 + H2O
H2CO3
-
-
-
?
CO2 + H2O
H2CO3
-
-
-
?
CO2 + H2O
H2CO3
-
among the seven known isozymes carbonic anhydrase III is the least efficient in catalytic hydration of CO2
-
r
CO2 + H2O
H2CO3
roles for residues 7, 62, and 67 in finetuning the properties of His64 for optimal proton transfer in catalysis
-
-
?
CO2 + H2O
H2CO3
-
kinetics of SspCA is characterized in terms of first order CO2 hydration rate according to a procedure based on CO2 absorption tests in a stirred cell apparatus
-
-
?
CO2 + H2O
H2CO3
-
kinetics of SspCA is characterized in terms of first order CO2 hydration rate according to a procedure based on CO2 absorption tests in a stirred cell apparatus
-
-
?
H2CO3
CO2 + H2O
-
plays a role in various physiological functions, including interconversion between CO2 and HCO3- in intermediary metabolism, facilitated diffusion of CO2, pH homeostasis and ion transport
-
r
H2CO3
CO2 + H2O
bicarbonate binding mode and binding structure, overview
-
-
r
H2CO3
CO2 + H2O
-
CsoSCA converts HCO3- to CO2 for use in carbon fixation by ribulose-bisphosphate carboxylase/oxygenase
-
-
?
H2CO3
CO2 + H2O
-
essential physiological function is to catalyze the hydration of carbon dioxide and the backreaction, the dehydration of bicarbonate
-
r
H2CO3
CO2 + H2O
-
the proton transfer from a zinc-bound water molecule to the proton shuttle His64, along a hydrogen-bonded water network, limits the reaction velocity of CO2 hydration. The side chain of His64 occupies two conformations in wild-type HCA II, pointing inward toward the zinc or outward toward bulk solvent. The enzyme shows a significant extension of the effective active site of HCA II from the zinc-bound water at the base of the conical cavity in the enzyme to Lys170 near the rim of the cavity
-
-
r
H2CO3
CO2 + H2O
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
-
-
r
H2CO3
CO2 + H2O
plays a role in the hypersensitive defense response
-
r
additional information
?
-
-
the enzyme shows esterase activity with 4-nitrophenyl acetate
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
recombinant engineered enzyme ASCA exhibits esterase activity with 4-nitrophenyl acetate and can promote CO2 absorption in an alkaline solvent required for efficient carbon capture. Recombinant mASCA is capable of catalyzing the conversion of CO2 to CaCO3 (calcite form) in the presence of Ca2+. The CO2 hydration activity is determined by monitoring the time required for the pH of the assay solution to change from 8.3 to 7.0 and using the formula [[(t0 - tc)/tc]/protein(mg)] [Wilbur-Anderson units (WAU) per mg of protein]
-
-
?
additional information
?
-
-
recombinant engineered enzyme ASCA exhibits esterase activity with 4-nitrophenyl acetate and can promote CO2 absorption in an alkaline solvent required for efficient carbon capture. Recombinant mASCA is capable of catalyzing the conversion of CO2 to CaCO3 (calcite form) in the presence of Ca2+. The CO2 hydration activity is determined by monitoring the time required for the pH of the assay solution to change from 8.3 to 7.0 and using the formula [[(t0 - tc)/tc]/protein(mg)] [Wilbur-Anderson units (WAU) per mg of protein]
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the enzyme is also active in an esterase assay with 4-nitrophenylacetate as substrate
-
-
?
additional information
?
-
-
other carbonic anhydrase isoforms than the well-characterized betaCA1 may contribute to the CO2 transfer in the cell to the catalytic site of ribulose 1,5-bisphosphate carboxylase/oxygenase
-
-
?
additional information
?
-
-
other carbonic anhydrase isoforms than the well-characterized betaCA1 may contribute to the CO2 transfer in the cell to the catalytic site of ribulose 1·5-bisphosphate carboxylase/oxygenase
-
-
?
additional information
?
-
-
BCA II when incubated under mildly denaturing condition of GdnHCl concentration of 1.5 M and a pH of 3.5 (slightly below its isoelectric point), forms ordered aggregates that are characteristically distinct from amorphous aggregates
-
-
?
additional information
?
-
enzyme activity assay with 4-nitrophenyl acetate as substrate using the enzyme's esterase activity
-
-
?
additional information
?
-
-
esterase activity with umbelliferone acetate
-
-
?
additional information
?
-
-
esterase activity with fluorescein diacetate, erythrocyte carbonic anhydrase II, no activity with cat caecum enzyme and erythrocyte carbonic anhydrase I
-
-
?
additional information
?
-
-
weak esterase activity with p-nitrophenyl acetate
-
-
?
additional information
?
-
-
carbonic anhydrase 2 is induced by high CO2 concentration, carbonic anhydrase 1 is induced by low and high CO2 concentration
-
-
?
additional information
?
-
-
the enzyme is induced by low CO2 conditions, the enzyme probably has an important role in adaption of this algal cell to low CO2 conditions. A possible role for the mitochondrial enzyme might be to function as a pH stabilizer to prevent alkalinization of the mitochondrial matrix at the onset of photorespiration. The enzyme could also be involved in the diffusion and transport of inorganic carbon species within the mitochondrial matrix as well as their efflux
-
-
?
additional information
?
-
-
external carbonic anhydrase enables algal cells to utilize HCO3- as inorganic carbon source in case that CO2 is limited externally to the plasma membrane
-
-
?
additional information
?
-
the enzyme shows a significant catalytic activity for the physiologic reaction of CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
-
the enzyme shows a significant catalytic activity for the physiologic reaction of CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
Colwellia psychrerythraea 34H / ATCC BAA-681
the enzyme shows a significant catalytic activity for the physiologic reaction of CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
enzyme TweCA has no esterase activity with 4-nitrophenyl acetate as substrate, measurement of CO2 hydration reaction for determination of enzyme activity by stopped-flow pH-based assay with bromothymol blue as indicator
-
-
?
additional information
?
-
-
enzyme TweCA has no esterase activity with 4-nitrophenyl acetate as substrate, measurement of CO2 hydration reaction for determination of enzyme activity by stopped-flow pH-based assay with bromothymol blue as indicator
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the enzyme also shows esterase activity with 4-nitrophenylacetate as substrate
-
-
?
additional information
?
-
-
the enzmye shows esterase activity with 4-nitrophenyl phosphate
-
-
?
additional information
?
-
stopped flow CO2 hydrase assay method
-
-
?
additional information
?
-
-
esterase activity with fluorescein diacetate, erythrocyte carbonic anhydrase II, no activity with cat caecum enzyme and erythrocyte carbonic anhydrase I
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
type II beta-carbonic anhydrases have a characteristic triad of non-catalytic residues, i.e. Trp39, Arg64, and Tyr181 in HICA, about 8 A away from the active site zinc ion that can bind bicarbonate ion. The studied anion binding site along the dimerization interface of HICA is an escort site that represents an intermediate along the ingress/egress route of bicarbonate ion to/from the allosteric binding site, overview. The mechanism of sulfate activation of HICA is the result of sulfate ion competing for bicarbonate at this escort site, preventing passage of bicarbonate from bulk solution to its allosteric site. The noncatalytic bicarbonate ion is a negative allosteric effector that stabilizes an inactive, T-state conformation of the enzyme, where Asp44 displaces the catalytically essential zinc-bound water. Type II beta-CAs can also adopt an active, R-state conformation in which Asp44 pairs with Arg46, allowing the coordination of the catalytically essential water molecule to the active site zinc ion. The noncatalytic bicarbonate ion stabilizes the inactive T state. The steric bulk of the Val47 side chain displaces bicarbonate from the allosteric binding site in the R state, and thus provides the necessary steric coupling mechanism between the bicarbonate binding and the adopted allosteric state
-
-
?
additional information
?
-
-
type II beta-carbonic anhydrases have a characteristic triad of non-catalytic residues, i.e. Trp39, Arg64, and Tyr181 in HICA, about 8 A away from the active site zinc ion that can bind bicarbonate ion. The studied anion binding site along the dimerization interface of HICA is an escort site that represents an intermediate along the ingress/egress route of bicarbonate ion to/from the allosteric binding site, overview. The mechanism of sulfate activation of HICA is the result of sulfate ion competing for bicarbonate at this escort site, preventing passage of bicarbonate from bulk solution to its allosteric site. The noncatalytic bicarbonate ion is a negative allosteric effector that stabilizes an inactive, T-state conformation of the enzyme, where Asp44 displaces the catalytically essential zinc-bound water. Type II beta-CAs can also adopt an active, R-state conformation in which Asp44 pairs with Arg46, allowing the coordination of the catalytically essential water molecule to the active site zinc ion. The noncatalytic bicarbonate ion stabilizes the inactive T state. The steric bulk of the Val47 side chain displaces bicarbonate from the allosteric binding site in the R state, and thus provides the necessary steric coupling mechanism between the bicarbonate binding and the adopted allosteric state
-
-
?
additional information
?
-
Halalkalibacterium halodurans
mineralization of CO2 using recombinant BhCA leads to accelerated precipitation of CaCO3 in calcite form. Recombinant BhCA also functions as an efficient virtual peroxidase when Zn2+ is substituted with Mn2+
-
-
?
additional information
?
-
Halalkalibacterium halodurans
the enzyme effectively sequesters CO2 into calcite form of CaCO3
-
-
?
additional information
?
-
Halalkalibacterium halodurans TSLV1
mineralization of CO2 using recombinant BhCA leads to accelerated precipitation of CaCO3 in calcite form. Recombinant BhCA also functions as an efficient virtual peroxidase when Zn2+ is substituted with Mn2+
-
-
?
additional information
?
-
Halalkalibacterium halodurans TSLV1 / MTCC 10961
the enzyme effectively sequesters CO2 into calcite form of CaCO3
-
-
?
additional information
?
-
-
esterase activity assay with 4-nitrophenyl acetate as substrate and measurement of CO2 hydration reaction for determination of enzyme activity
-
-
?
additional information
?
-
-
rCsoSCA exhibits no detectable esterase activity when assayed spectrophotometrically with 4-nitrophenylacetate as a substrate
-
-
?
additional information
?
-
-
carbonic anhydrase I, II and III are constitutive enzymes
-
-
?
additional information
?
-
-
carbonic anhydrase IV is possibly responsible for HCO3- secretion, the cytoplasmic form of carbonic anhydrase II is believed to play a role in pH regulation near apical ionic channels of the near apical carbonic anhydrase IV
-
-
?
additional information
?
-
carbonic anhydrase II increases the activity of the human electrogenic Na+/HCO3- cotransporter
-
-
?
additional information
?
-
-
carbonic anhydrase II increases the activity of the human electrogenic Na+/HCO3- cotransporter
-
-
?
additional information
?
-
extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation
-
-
?
additional information
?
-
-
extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation
-
-
?
additional information
?
-
-
the enzyme also shows esterase activity in 4-nitrophenylacetate hydrolysis
-
-
?
additional information
?
-
-
the enzyme also shows esterase activity in 4-nitrophenylacetate hydrolysis
-
-
?
additional information
?
-
-
the enzyme shows esterase assay with 4-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
4-nitrophenyl acetate is used as the substrate to measure the activity of enzyme CAVA
-
-
?
additional information
?
-
-
4-nitrophenyl acetate is used as the substrate to measure the activity of enzyme CAVA
-
-
?
additional information
?
-
determination of enzyme esterase activity using p-nitrophenyl acetate as substrate. Presence of D2O reduces catalysis, but does not change how it proceeds
-
-
?
additional information
?
-
determination of enzyme esterase activity using p-nitrophenyl acetate as substrate. Presence of D2O reduces catalysis, but does not change how it proceeds
-
-
?
additional information
?
-
-
determination of enzyme esterase activity using p-nitrophenyl acetate as substrate. Presence of D2O reduces catalysis, but does not change how it proceeds
-
-
?
additional information
?
-
enzyme activity measurement by determining the enzyme's esterase activity with substrate 4-nitrophenyl acetate
-
-
?
additional information
?
-
enzyme activity measurements determining CO2-hydratase activity or determining esterase activity with 4-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
enzyme activity measurements determining CO2-hydratase activity or determining esterase activity with 4-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
-
enzyme activity measurements determining CO2-hydratase activity or determining esterase activity with 4-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
enzyme activity measurements determining CO2-hydratase activity or determining esterase activity with 4-nitrophenylacetate as substrate
-
-
?
additional information
?
-
enzyme activity measurements determining CO2-hydratase activity or determining esterase activity with 4-nitrophenylacetate as substrate
-
-
?
additional information
?
-
-
enzyme activity measurements determining CO2-hydratase activity or determining esterase activity with 4-nitrophenylacetate as substrate
-
-
?
additional information
?
-
esterase activity assay with 4-nitrophenyl acetate as substrate for determination of activity of wild-type and mutant enzymes
-
-
?
additional information
?
-
reactivity of the purified CA XIV is determined by following the CO2 hydration using the stopped-flow technique
-
-
?
additional information
?
-
-
reactivity of the purified CA XIV is determined by following the CO2 hydration using the stopped-flow technique
-
-
?
additional information
?
-
-
the carbonic anhydrase enzyme activity is measured by the pH change of 0.02 M Tris buffer. The reaction is initiated by the addition of substrate and the time needed for the pH of the reaction mixture to drop from pH 8.3 to pH 6.3 is recorded
-
-
?
additional information
?
-
-
that carbonic anhydrase domain in alcyonarian is involved in the calcification process
-
-
?
additional information
?
-
-
no esterase activity detected with p-phenylacetate as the substrate
-
?
additional information
?
-
stopped-flow enzyme assay
-
-
?
additional information
?
-
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
stopped-flow enzyme assay
-
-
?
additional information
?
-
the enzyme is involved in various physiological processess such as acid-base balance and transport of CO2 and ions
-
-
?
additional information
?
-
-
the enzyme is involved in various physiological processess such as acid-base balance and transport of CO2 and ions
-
-
?
additional information
?
-
-
carbonic anhydrase IV mediates buffering in the extracellular space in central nervous system
-
-
?
additional information
?
-
-
carbonic anhydrase XIV may facilitate CO2 removal from neural retina and modulate photoreceptor function
-
-
?
additional information
?
-
-
carbonic anhydrase XIV mediates buffering in the extracellular space in central nervous system
-
-
?
additional information
?
-
the renal carbonic anhydrase type III plays a role in proximal tubule dysfunction
-
-
?
additional information
?
-
enzyme activity measurement by stopped-flow CO2 hydrase assay
-
-
?
additional information
?
-
-
enzyme activity measurement by stopped-flow CO2 hydrase assay
-
-
?
additional information
?
-
enzyme activity measurement by stopped-flow CO2 hydrase assay
-
-
?
additional information
?
-
enzyme activity measurement by stopped-flow CO2 hydrase assay
-
-
?
additional information
?
-
4-nitrophenylacetate is used as activity assay substrate
-
-
?
additional information
?
-
-
4-nitrophenylacetate is used as activity assay substrate
-
-
?
additional information
?
-
-
esterase activity with p-nitrophenyl acetate
-
-
?
additional information
?
-
-
esterase activity with p-nitrophenyl acetate
-
-
?
additional information
?
-
-
weak esterase activity with p-nitrophenyl acetate
-
-
?
additional information
?
-
-
weak esterase activity with p-nitrophenyl acetate
-
-
?
additional information
?
-
-
the enzyme has significant catalytic activity for the physiologic reaction, CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
-
the enzyme is highly active in the CO2 hydration reaction
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the Na+/H+ antiporter NHE1 is the major exporter of protons by skeletal muscle in recovery from a period of anoxia. It is essential for functioning carbonic anhydrase to be attached to NHE1 to activate it
-
-
?
additional information
?
-
-
enzyme esterase activity assay using p-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
-
enzyme esterase activity assay using p-nitrophenylacetate as substrate
-
-
?
additional information
?
-
Ovis aries Kangal Akkaraman
-
enzyme esterase activity assay using p-nitrophenylacetate as substrate
-
-
?
additional information
?
-
Ovis aries Kangal Akkaraman
-
enzyme esterase activity assay using p-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
activity measurement by colorimetric reaction with P-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
-
activity measurement by colorimetric reaction with P-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
enzyme activity measurement by determining the enzyme's CO2 hydration activity and esterase activity with substrate 4-nitrophenyl acetate. The recombinant enzyme lacking the signal peptide can efficiently catalyze the hydration of CO2, precipitating CaCO3 as calcite in the presence of Ca2+
-
-
?
additional information
?
-
Persephonella marina DSM 14350 / EX-H1
enzyme activity measurement by determining the enzyme's CO2 hydration activity and esterase activity with substrate 4-nitrophenyl acetate. The recombinant enzyme lacking the signal peptide can efficiently catalyze the hydration of CO2, precipitating CaCO3 as calcite in the presence of Ca2+
-
-
?
additional information
?
-
-
rn the erythrocyte, carbonic anhydrase is necessary to facilitate the transport of carbon dioxide out of the body
-
-
?
additional information
?
-
the enzyme has a medium-low catalytic activity for the physiologic reaction of CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
-
carbonic anhydrase does not influence the fast contractile kinetics characteristic of the extraocular muscles
-
-
?
additional information
?
-
-
enzyme activity assay using the enzyme's esterase activity with 4-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
Salmo trutta Labrax Coruhensis
-
enzyme assay with 4-nitrophenyl acetate as substrate
-
-
?
additional information
?
-
enzyme SazCA is highly active in the CO2 hydration reaction
-
-
?
additional information
?
-
-
enzyme SazCA is highly active in the CO2 hydration reaction
-
-
?
additional information
?
-
-
the enzyme shows very high activity compared to other carbonic anhydrases, it has also esterase activity
-
-
?
additional information
?
-
Sulfurihydrogenibium azorense Az-Fu1 / DSM 15241 / OCM 825
enzyme SazCA is highly active in the CO2 hydration reaction
-
-
?
additional information
?
-
the enzyme also presents esterase activity
-
-
?
additional information
?
-
CcaA-CcmM interactions, overview
-
-
?
additional information
?
-
Synechocystis sp. PCC 6803 / Kazusa
protein/protein-binding analysis with recombinant enzyme variants CcaA220 and CcaA274 using surface plasmon resonance. CcaA-CcmM interactions, overview
-
-
?
additional information
?
-
-
in mortality bioassays, carbonic anhydrase protects Tribolium castaneum from the toxicity of COS but has the opposite effect on COS toxicity. With CS2, carbonic anhydrase has a very minor role, neither facilitating, nor protecting against toxicity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CO2 + H2O
H2CO3
-
periplasmic alpha-carbonic anhydrase activity of Helicobacter pylori is essential for acid acclimation
-
-
?
H2CO3
CO2 + H2O
-
plays a role in various physiological functions, including interconversion between CO2 and HCO3- in intermediary metabolism, facilitated diffusion of CO2, pH homeostasis and ion transport
-
r
H2CO3
CO2 + H2O
-
CsoSCA converts HCO3- to CO2 for use in carbon fixation by ribulose-bisphosphate carboxylase/oxygenase
-
-
?
H2CO3
CO2 + H2O
-
essential physiological function is to catalyze the hydration of carbon dioxide and the backreaction, the dehydration of bicarbonate
-
r
H2CO3
CO2 + H2O
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
-
-
r
H2CO3
CO2 + H2O
plays a role in the hypersensitive defense response
-
r
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
other carbonic anhydrase isoforms than the well-characterized betaCA1 may contribute to the CO2 transfer in the cell to the catalytic site of ribulose 1,5-bisphosphate carboxylase/oxygenase
-
-
?
additional information
?
-
-
other carbonic anhydrase isoforms than the well-characterized betaCA1 may contribute to the CO2 transfer in the cell to the catalytic site of ribulose 1·5-bisphosphate carboxylase/oxygenase
-
-
?
additional information
?
-
-
BCA II when incubated under mildly denaturing condition of GdnHCl concentration of 1.5 M and a pH of 3.5 (slightly below its isoelectric point), forms ordered aggregates that are characteristically distinct from amorphous aggregates
-
-
?
additional information
?
-
-
carbonic anhydrase 2 is induced by high CO2 concentration, carbonic anhydrase 1 is induced by low and high CO2 concentration
-
-
?
additional information
?
-
-
the enzyme is induced by low CO2 conditions, the enzyme probably has an important role in adaption of this algal cell to low CO2 conditions. A possible role for the mitochondrial enzyme might be to function as a pH stabilizer to prevent alkalinization of the mitochondrial matrix at the onset of photorespiration. The enzyme could also be involved in the diffusion and transport of inorganic carbon species within the mitochondrial matrix as well as their efflux
-
-
?
additional information
?
-
-
external carbonic anhydrase enables algal cells to utilize HCO3- as inorganic carbon source in case that CO2 is limited externally to the plasma membrane
-
-
?
additional information
?
-
the enzyme shows a significant catalytic activity for the physiologic reaction of CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
-
the enzyme shows a significant catalytic activity for the physiologic reaction of CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
Colwellia psychrerythraea 34H / ATCC BAA-681
the enzyme shows a significant catalytic activity for the physiologic reaction of CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 1 carries out nonphotosynthetic functions, including lipid biosynthesis and antioxidant activity
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 3 is responsible for catalyzing the first step in the C4 pathway in the mesophyll cell cytosol
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
carbonic anhydrase 2 provides bicarbonate for anapleurotic reactions involving nonphotosynthetic forms of phosphoenol pyruvate carboxylase in the cytosol of cells in both photosynthetic and nongreen tissues
-
-
?
additional information
?
-
-
carbonic anhydrase I, II and III are constitutive enzymes
-
-
?
additional information
?
-
-
carbonic anhydrase IV is possibly responsible for HCO3- secretion, the cytoplasmic form of carbonic anhydrase II is believed to play a role in pH regulation near apical ionic channels of the near apical carbonic anhydrase IV
-
-
?
additional information
?
-
carbonic anhydrase II increases the activity of the human electrogenic Na+/HCO3- cotransporter
-
-
?
additional information
?
-
-
carbonic anhydrase II increases the activity of the human electrogenic Na+/HCO3- cotransporter
-
-
?
additional information
?
-
extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation
-
-
?
additional information
?
-
-
extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation
-
-
?
additional information
?
-
-
that carbonic anhydrase domain in alcyonarian is involved in the calcification process
-
-
?
additional information
?
-
the enzyme is involved in various physiological processess such as acid-base balance and transport of CO2 and ions
-
-
?
additional information
?
-
-
the enzyme is involved in various physiological processess such as acid-base balance and transport of CO2 and ions
-
-
?
additional information
?
-
-
carbonic anhydrase IV mediates buffering in the extracellular space in central nervous system
-
-
?
additional information
?
-
-
carbonic anhydrase XIV may facilitate CO2 removal from neural retina and modulate photoreceptor function
-
-
?
additional information
?
-
-
carbonic anhydrase XIV mediates buffering in the extracellular space in central nervous system
-
-
?
additional information
?
-
the renal carbonic anhydrase type III plays a role in proximal tubule dysfunction
-
-
?
additional information
?
-
-
the enzyme has significant catalytic activity for the physiologic reaction, CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
-
the enzyme might play a key role in maintenance of midgut pH
-
-
?
additional information
?
-
-
the Na+/H+ antiporter NHE1 is the major exporter of protons by skeletal muscle in recovery from a period of anoxia. It is essential for functioning carbonic anhydrase to be attached to NHE1 to activate it
-
-
?
additional information
?
-
-
rn the erythrocyte, carbonic anhydrase is necessary to facilitate the transport of carbon dioxide out of the body
-
-
?
additional information
?
-
the enzyme has a medium-low catalytic activity for the physiologic reaction of CO2 hydration to bicarbonate and protons
-
-
?
additional information
?
-
-
carbonic anhydrase does not influence the fast contractile kinetics characteristic of the extraocular muscles
-
-
?
additional information
?
-
enzyme SazCA is highly active in the CO2 hydration reaction
-
-
?
additional information
?
-
-
enzyme SazCA is highly active in the CO2 hydration reaction
-
-
?
additional information
?
-
Sulfurihydrogenibium azorense Az-Fu1 / DSM 15241 / OCM 825
enzyme SazCA is highly active in the CO2 hydration reaction
-
-
?
additional information
?
-
-
in mortality bioassays, carbonic anhydrase protects Tribolium castaneum from the toxicity of COS but has the opposite effect on COS toxicity. With CS2, carbonic anhydrase has a very minor role, neither facilitating, nor protecting against toxicity
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Co2+
Cu2+
Fe2+
KCl
enzyme retains activity at salt concentrations ranging from low salt to at least 1.5 M NaCl or KCl for CO2 hydration, 2.0 M NaCl for esterase activity and 0.5 M for bicarbonate dehydration
Mg2+
Mn2+
Na+
a key role for sodium ions in increasing halotolerant enzyme stability largely through interactions with the highly ordered first Na+ hydration shell, molecular dynamics calculations, overview. Very strong activation by Na2SO4 of all enzymes, especially of mutant M4, slight activation by NaCl, overview
NaCl
enzyme retains activity at salt concentrations ranging from low salt to at least 1.5 M NaCl or KCl for CO2 hydration, 2.0 M NaCl for esterase activity and 0.5 M for bicarbonate dehydration
Ni2+
Sn2+
SO42-
sulfate
the sulfate ion competes with the bicarbonate ion for the binding site near the active site affecting the allosteric regulation of the enzyme, binding structure in wild-type an dmutant enzymes, overview
Zinc
Zn2+
additional information
Cd2+
-
replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme
Cd2+
-
replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme
Co2+
-
preparation of a Co(II)-substituted HICA, Co-HICA. Co(II)-substituted HICA, Co-HICA, has comparable, 20% enhanced kcat and 2.3fold increased Km/kcat compared to that of the wild-type enzyme
Co2+
strongly activating effect, Co2+ induces an increase in the kcat/Km value
Co2+
removal of Zn2+ and preparation of Co(II)-substituted carbonic anhydrase II, Co(II)-HCA II. Change in metal coordination from tetrahedral at pH 11.0 to a coordination consistent with a mixed population of both tetrahedral and penta-coordinate at pH 8.5 to an octahedral geometry characteristic of the oxidized enzyme Co(III)-HCA II at pH 6.0
Co2+
Macropus eugenii desmarest
-
when added back to the apoenzyme in a 1:1 molar ratio or greater, the activity immediately returns to control level
Co2+
-
activates to a 2fold activity compared to the activity with Zn2+
Fe2+
-
contains one iron ion per monomer when synthesized in Methanosarcina acetivorans
Fe2+
anaerobic reconstitution of apoenzyme with Fe2+, which yields an enzyme with an effective kcat that exceeds that for the Zn2+-reconstituted enzyme. The Fe2+-reconstituted enzyme contains high spin Fe2+ that, when oxidized to Fe3+, inactivates the enzyme. Reconstitution with Fe3+ is unsuccessful
Fe2+
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme. The Fe2+-reconstituted enzyme contains high spin Fe2+ that, when oxidized to Fe3+, inactivates the enzyme. Reconstitution with Fe3+ is unsuccessful
Fe2+
the homotrimer purified from Escherichia coli cultured with supplemental zinc contains 0.71 zinc and 0.15 iron per monomer. Enzyme purified from Escheria coli cultured with supplemental iron contains 0.15 iron per monomer and only a trace amount of zinc
Fe2+
-
when overproduced in Escherichia coli or in Methanosarcina acetivorans and subsequently anaerobically purified, the enzyme contains Fe2+ in the active site and is 4fold more active. In these conditions, catalytic activity is rapidly lost after exposure to air, as a consequence of the oxidation of Fe2+ to Fe3+ and loss of the metal from the active site, thus convincing evidence is that iron is the physiologically relevant metal for this enzyme
Mg2+
strongly activating effect, Mg2+ induces an increase in the kcat/Km value
Mn2+
Halalkalibacterium halodurans
BhCA also functions as an efficient virtual peroxidase when Zn2+ is substituted with Mn2+
Mn2+
strongly activating effect, Mn2+ induces an increase in the kcat/Km value
SO42-
Halalkalibacterium halodurans
the recombinant enzyme displays the unique property of stimulation in presence of SO42-
Zinc
-
the major enzyme form contains 1 gatom of zinc per 30000 Da enzyme, the minor enzyme form contains 1.09 gatom of zinc per 30000 Da enzyme
Zinc
-
the Zn2+ enzyme remains essentially fourcoordinate in all its forms, although alterations in the K-edge shape imply differences in coordination geometry
Zinc
Macropus eugenii desmarest
-
Zn2+, when added back to the apoenzyme in a 1:1 molar ratio or greater, the activity immediately returns to control level
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
required, carbonic anhydrase is a metalloenzyme, that binds a single zinc atom in its active site using three histidine ligands. The enzyme binds zinc relatively strongly with an apparent stability constant (log(KF)) of approximately 11.4 at pH 7.0. Following de novo protein synthesis, apocarbonic anhydrase must acquire and insert the enzymatically necessary zinc atom into the active site. The enzyme accepts donation of a single zinc atom from zinc-saturated metallothioneins at rates and concentrations that supports in vivo zinc donation by metallothionein (MT), fully saturated Zn-MT is capable of donating zinc to the apoenzyme. Competitive zinc titration to a solution containing equal concentrations of apo-rhMT1A and apoCA, formation of the fully metalated Zn7MT and holo-ZnCA, kinetics, simulation and modelling, overview
Zn2+
beta class CAs contain four protein zinc ligands, one His, two Cys, and one Asp coordinated to Zn(II). At pH 8.0, no water is coordinated to the metal ion
Zn2+
-
required, isozymes CAH-3, CAH-4 and CAH-5 contain the three zinc-binding histidines that are important for enzyme activity, His94, His96, and His119, and also two ligands that provide a hydrogen bond to stabilize the zinc ion during catalysis, Gln-92 and Glu-117
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
required, metalloenzyme. The three amino acid residues Asn73, Gln75 and Asn202, which constitute the triad involved in the network of hydrogen bonds with the zinc-coordinated water molecule, are conserved in all the sequences of gamma-CA enzymes. The enzyme CpsCA trimer contains 3 active sites and each monomer contributes His residues located on the surface to coordinate the Zn(II) ion crucial for catalysis
Zn2+
-
Cd2+ can be substituted by Zn2+, yielding an even more efficient enzyme
Zn2+
-
required for activity. Replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
required, metalloenzyme, the catalytic residues Asp44 and Arg46 are involved in activation of the zinc-coordinated water molecule/hydroxide ion for catalysis
Zn2+
-
required, increases the growth rate of the cells and the enzyme activity
Zn2+
-
addition of 1 mM ZnCl2 to the metal-depleted enzyme restores the ctivity to nearly the level observed for nondialyzed samples, while neither CoCl2 nor MgCl2 is able to reverse the inactivation of the enzyme. Zn2+ contents of 0.9 mol of Zn2+ per mol of monomer
Zn2+
-
-
Zn2+
strongly activating effect, the recombinant extracellular domain of CA IX, which includes both the proteoglycan and catalytic domains, shows 2166% increase of activity in the presence of 0.05 mM Zn2+
Zn2+
-
required for catalysis, the side chain of His64 occupies two conformations in wild-type HCA II, pointing inward toward the zinc or outward toward bulk solvent
Zn2+
-
required. The side chain of Tyr7 in HCA II extends into the active-site cavity about 7 A from the catalytic zinc atom
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
required, metalloenzyme, molecular dynamics simulations in catalysis. Active site residues correspond to His94, His96, His119 belonging to the inner coordination shell of the metal ion and Glu106, Thr199, Thr200 belonging to the outer one
Zn2+
required, metalloenzyme, residues His130, His132, and His155 are zinc iron binding sites
Zn2+
-
contains one zinc ion per monomer when overproduced in Escherichia coli
Zn2+
-
required for activity. Replacement of zinc ion with cadmium does not entail significant differences in the catalytic performance of the enzyme
Zn2+
the homotrimer purified from Escherichia coli cultured with supplemental zinc contains 0.71 zinc and 0.15 iron per monomer. Enzyme purified from Escherichia coli cultured with supplemental iron contains 0.15 iron per monomer and only a trace amount of zinc
Zn2+
-
the individual subunits are only weakly folded and fractionally associated in the absence of Zn2+. The crucial thermodynamic step in the assembly of the trimeric holo-Cam is the incorporation of the three Zn2+ ions, events which must occur after the monomer is resident on the surface and has access to other monomers
Zn2+
-
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues. Each monomer of the enzyme dimer contains a zinc ion tetrahedrally coordinated by two cysteines (Cys32 and Cys90), one histidine (His87) and a water molecule/hydroxide ion
Zn2+
the conserved three histidines, His94, His96, and His119 (hCA I numbering system) coordinate the Zn(II) ion that is crucial for catalysis
Zn2+
the metalloenzyme, the Zn(II) ion is crucial for catalysis, the enzyme sequence contains the three His residues acting as zinc ligands
Zn2+
-
addition of zinc improves the CO2 hydration activity of the rice CA produced by Escherichia coli
Zn2+
required, metalloenzyme, three histidine residues predicted to form the Zn2+ coordination center, H233, H235, and H258, are conserved in Pl-CAN
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
required, metalloenzyme, activates the recombinant enzyme lacking the signal peptide
Zn2+
required, metalloenzyme. The zinc ion is coordinated by residues His299, His301 and Gln320
Zn2+
zinc-containing metalloenzyme, the asymmetric unit contains a catalytic Zn2+ ion
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
a zinc ion is coordinated by the three highly conserved residues Cys57, His112 and Cys115
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
-
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
required, metalloenzyme, on the bottom of a central cavity, the catalytic zinc ion is tetrahedrally coordinated by the three histidine residues (His89, His91 and His108)
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three histidine residues: His89, His91 and His108, zinc cordination site structure, PDB ID 4G7A
Zn2+
Synechocystis sp. PCC 6803 / Kazusa
required, metalloenzyme, the zinc ion bound to Cys39, His98, and Cys101 in the catalytic site, water forms the fourth zinc ligand
Zn2+
metalloenzyme, the metal ion is required for catalytic activity, coordinated by three residues
Zn2+
required, zinc enzyme, one of the Zn2+-containing active sites might be located externally and the other one inside the cell. Conserved histidine residues (His116, His118, His141) coordinate the Zn2+-containing catalytic site
additional information
-
the enzyme shows an optimum ionic strength at 10mM
additional information
Halalkalibacterium halodurans
no effect on enzyme activity at 5 mM by Ca2+, NH4+, Mg2+, Ba2+, and Mn2+
additional information
Halalkalibacterium halodurans
rBhCA activity is unaffected by Na+ and Cl- up to 1.0 M or by Pb2+ at 1 mM. rBhCA is able to tolerate high concentration of NO32- and SO32- up to 1 M without losing activity
additional information
-
the enzyme has an optimum ionic strength at 20 mM. Sulfate, sulfide, azide, nitrate, nitrite and iodide exhibit strong inhibitory activity in the micromolar range (Ki values of 5.5-15.5 mM). Cyanide, bromide, chloride, and carbonate are moderate inhibitors, whereas other anions show only weak activities
additional information
distribution of cations and anions within 3 A of the enzyme surface, overview
additional information
-
reconstitution of the apoenzyme with Cu2+, Mn2+, Ni2+, or Cd2+ yields enzymes with effective kcat values that are 10% or less than the value for the Zn2+-reconstituted apoenzyme
additional information
reconstitution of the apoenzyme with Cu2+, Mn2+, Ni2+, or Cd2+ yields enzymes with effective kcat values that are 10% or less than the value for the Zn2+-reconstituted apoenzyme
additional information
-
the metal ion in the enzyme isolated directly from Methanosarcina thermophila is not been determined since only enzyme overproduced in Escherichia coli is characterized
additional information
the metal ion in the enzyme isolated directly from Methanosarcina thermophila is not been determined since only enzyme overproduced in Escherichia coli is characterized
additional information
-
analysis of three-dimensional structures of MtCam, in both Zn- and Co-bound forms, overview. Structure comparisons
additional information
the recombinant enzyme activity is not affected significantly by the presence of Ca2+, Mg2+, or K+ ions
additional information
homology modeling analysis shows that the metal ion coordination pattern of the eta-CA involves two His and one Gln residues in addition to the water molecule/hydroxide ion acting as nucleophile in the catalytic cycle
additional information
-
homology modeling analysis shows that the metal ion coordination pattern of the eta-CA involves two His and one Gln residues in addition to the water molecule/hydroxide ion acting as nucleophile in the catalytic cycle
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
((3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis([1,3]dioxolo)[4,5-b:4',5'-d]pyran-3a-yl)methyl sulfamate
-
-
(1R,2S,3S,4S)-4,6-diamino-2-([3-O-[(1S,2S,3S,4S,5S)-2-amino-5-(aminomethyl)-3,4-dihydroxycyclohexyl]-alpha-L-arabinofuranosyl]oxy)-3-hydroxycyclohexyl 2,6-diamino-2,6-dideoxy-beta-L-glucopyranoside
-
i.e. neosym
(2E)-2-[(4-hydroxy-3-methylphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
-
(2E)-2-[(4-hydroxyphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
-
(2R)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
-
(2S)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
-
(2S,5R,6R)-3,3-dimethyl-7-oxo-6-(2-phenylacetamido)-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
-
i.e. penokain G
-
(2Z)-2-(2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
(2Z)-2-(4-fluorobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(4-methylpentan-2-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
(2Z)-2-(5-bromo-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl sulfamate
-
-
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-1,1-dioxo-1,2,3,4-tetrahydro-1lambda~6~-thieno[3,2-e][1,2]thiazine-6-sulfonamide
-
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
(4S,6S)-4-(ethylamino)-6-methyl-7,7-dioxo-4,5,6,7-tetrahydro-7lambda~6~-thieno[2,3-b]thiopyran-2-sulfonamide
-
(5Z)-2-amino-5-(4-hydroxy-3-methoxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
-
-
(6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
-
(7S)-7-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino]-3-[[(furan-2-carbonyl)sulfanyl]methyl]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
-
i.e. ceftiofur
(E)-3-phenyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)prop-2-en-1-one
-
36% inhibition
(R)- 4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
-
(R)-17(R)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
-
(R)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
-
(R)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(R)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
-
(R)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
-
(R)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
-
(R)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
-
(S)- 4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
-
(S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate
-
(S)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
-
(S)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
-
(S)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
-
(S)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
-
(S)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
-
(S)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
-
(S)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
-
(S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate
-
(S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate
-
(S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate
-
(S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate
-
(S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate
-
(S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate
-
1,1'-(trichloro-lambda5-stibanediyl)bis[2-amino-4,6-dimethoxy-5-[(1H-tetrazol-5-yl)sulfanyl]pyrimidin-1-ium]
14.3% inhibition of CO2 hydration reaction after 30 min
1,1-dimethyl-4-(7-sulfamoyl-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazol-3-yl)piperazin-1-ium iodide
-
1,3-dimethylpyrimidine-2,4(1H,3H)-dione
inhibition of isozyme hCA I; inhibition of isozyme hCA II
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
-
1-[2-(1H-imidazol-5-yl)ethyl]-4-methyl-2,6-di(propan-2-yl)pyridin-1-ium hexafluorophosphate
-
12,12,12-tribromo-7-oxo-6,7a,8,9,10,12-hexahydro-7H-12lambda5-pyrrolo[1',2':1,7][1,3,5,2]triazastibepino[4,3-b][1,3]benzothiazol-13-ium
2,3,4,5,6-pentafluoro-N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)benzamide
-
-
2,3,4,5,6-pentafluoro-N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]benzamide
-
-
2,3,6-trifluoro-4-(2-hydroxyethanesulfonyl)-5-[[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl]amino]benzene-1-sulfonamide
-
2-(1-methylethyl)-3-[(2-propynylamino)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-(1-methylethyl)-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-(2,2-dichloroacetylamino)-1,3,4-thiadiazole-5-sulfonamide
-
noncompetitive inhibition
2-(2-hydroxyethyl)-N-(1,1-dimethylethyl)-2H-thieno[3,2-e-]-1,2-thiazine-6-sulfonamide 1,1-dioxide
-
-
2-(2-methoxyethyl)-3-[(4-morpholinyl)methyl]-2-(2-propenyl)-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-(2-methoxyethyl)-3-[[bis(2-methoxyethyl)amino]methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-(3,4-dimethoxyphenyl)-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-(3-chloropropionylamino)-1,3,4-thiadiazole-5-sulfonamide
-
noncompetitive inhibition
2-(3-hydroxyphenyl)-3-(4-morpholinylmethyl)-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-(3-hydroxyphenyl)-3-[(2-propynylamino)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-(3-hydroxyphenyl)ethyl (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate
-
2-(3-hydroxyphenyl)ethyl (2E)-3-(4-hydroxyphenyl)prop-2-enoate
-
2-(3-hydroxypropyl)-3-(4-morpholinylmethyl)-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-(3-methoxyphenyl)-3-[(2-hydroxyethylamino)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-(3-methoxyphenyl)-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-(3-methoxypropyl)-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-(3-methoxypropyl)-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
2-(3-phenylpropionylamino)-1,3,4-thiadiazole-5-sulfonamide
-
noncompetitive inhibition
2-(4-hydroxyphenyl)ethyl (2E)-3-(3-hydroperoxy-4-hydroxyphenyl)prop-2-enoate
-
2-(4-hydroxyphenyl)ethyl (2E)-3-(4-hydroxyphenyl)prop-2-enoate
-
2-(benzenesulfonamido-N-benzyl)-5-[N,Ndibenzylsulfonamido]-l,3,4-thiadiazole
-
-
2-(hydroxymethyl)-4-nitro-N-[2-(4-sulfamoylphenyl)ethyl]benzene-1-sulfonamide
-
2-cyclohexyl-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-cyclopropylmethyl-3-[(4-morpholinyl)methyl]-2-(2-propenyl)-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-ethyl-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-ethyl-3-[[bis(2-hydroxyethyl)amino]methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-ethyl-3-[[bis(2-methoxyethyl)amino]methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-methyl-3-(4-morpholinylmethyl)-2H-thieno[2,3-e]-1,2-thiazine-6-sulfonamide 1,1-dioxide
-
-
2-methyl-3-(4-morpholinylmethyl)-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-methyl-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-methyl-3-[[N-(2-methoxyethyl)-N-(2-propenyl)amino]methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-methyl-3-[[N-(2-methoxyethyl)-N-(3-methoxypropyl)-amino]methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-propyl-3-[(2-propynylamino)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-[(4-methoxyphenyl)methyl]-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
2-[(4-methoxyphenyl)methyl]-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-[(4-morpholinyl)phenyl]-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
2-[(p-toluenesulfonamido)-N-methyl]-5-[N,N-dimethylsulfonamide]-l,3,4-thiadiazole
-
-
2-[2-(4-morpholinyl)ethyl]-2H-thieno[3,2-e-]-1,2-thiazine-6-sulfonamide 1,1-dioxide hydrochloride
-
-
2-[2-(acetoxy)ethyl]-N-(1,1-dimethylethyl)-4-hydroxy-2H-thieno[3,2-e-]-1,2-thiazine-6-sulfonamide 1,1-dioxide
-
-
2-[2-(propylamino)ethyl]-2H-thieno[3,2-e-]-1,2-thiazine-6-sulfonamide 1,1-dioxide hydrochloride
-
-
2-[2-[4-acetyl-(1-piperazinyl)]ethyl]-2H-thieno[3,2-e-]-1,2-thiazine-6-sulfonamide 1,1-dioxide
-
-
2-[2-[bis(2-methoxyethyl)amino]ethyl]-2H-thieno[3,2-e-]-1,2-thiazine-6-sulfonamide 1,1-dioxide hydrochloride
-
-
2-[3-[2-(3-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
-
2-[4-(4-morpholinyl)-2-butenyl]-2H-thieno[3,2-e-]-1,2-thiazine-6-sulfonamide 1,1-dioxide hydrochloride
-
-
2-[4-[2-(4-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
-
2-[[(5-chlorothiophen-2-yl)(hydroxy)methyl]amino]-1-(trichloro[2-[2-(5-chlorothiophen-2-yl)-2-oxoethyl]pyrimidin-1-ium-1-yl]-lambda5-stibanyl)pyrimidin-1-ium
3-(4-methylpiperazin-1-yl)-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
-
3-(benzylamino)-2,5,6-trifluoro-4-(2-hydroxyethanesulfonyl)benzene-1-sulfonamide
-
3-(methylsulfanyl)-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
-
3-(methylsulfonyl)-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
-
3-(phenylsulfanyl)-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
-
3-amino-1,1,1-tribromo-4,5-dihydro-1H-1lambda5-[1,3,5,2]triazastibinino[1,6-a]benzimidazol-10-ium
35% inhibition of CO2 hydration reaction after 30 min
3-amino-1,1,1-trichloro-4,5-dihydro-1H-1lambda5-[1,3,5,2]triazastibinino[1,6-a]benzimidazol-10-ium
10.0% inhibition of CO2 hydration reaction after 30 min
3-chloromethyl-N-(1,1-dimethylethyl)-2-(3-methoxyphenyl)-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
3-hydroxymethyl 2-methyl-2H-thieno[2,3-e]-1,2-thiazine-6-sulfonamide 1,1-dioxide
-
-
3-hydroxymethyl-2-methyl-2H-thieno[3,2-e]-1,2-thiazine-6-sulfonamide 1,1-dioxide
-
-
3-methylsalicylic acid
-
noncompetitive inhibition of isozyme carbonic anhydrase I and uncompetitive inhibition of isozyme carbonic anhydrase II
3-morpholin-4-yl-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
-
3-[(1-imidazolyl)methyl]-2-(3-methoxypropyl)-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
3-[(4-morpholinyl)methyl]-2-(2-propenyl)-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
3-[(4-morpholinyl)methyl]-2-propyl-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
3-[(cyclopropylamino)methyl]-2-(3-methoxypropyl)-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
3-[[(1S)-2,3-dihydro-1H-inden-1-yl]amino]-2,5,6-trifluoro-4-(2-hydroxyethanesulfonyl)benzene-1-sulfonamide
-
3-[[(1S)-2,3-dihydro-1H-inden-1-yl]amino]-2,5,6-trifluoro-4-(2-phenylethanesulfonyl)benzene-1-sulfonamide
-
3-[[(3,4-dimethoxyphenyl)methyl]amino]-2,5,6-trifluoro-4-(2-hydroxyethanesulfonyl)benzene-1-sulfonamide
-
3-[[bis(2-methoxyethyl)amino]methyl]-2-propyl-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
3-[[N-(2-methoxyethyl)-N-(2-propenyl)amino]methyl]-2-methyl-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
3-[[N-(2-methoxyethyl)-N-(3-methoxypropyl)amino]methyl]-2-methyl-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide hydrochloride
-
-
3-[[N-(2-methoxyethyl)-N-methylamino]methyl]-2-methyl-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
4,6-dinitrosalicylic acid
-
noncompetitive inhibition of isozymes carbonic anhydrase I and II
4-(3,4-dichlorophenylureido)thioureido-benzenesulfonamide
-
effective in vitro carbonic anhydrase inhibitor
4-(3-[[(1E)-(1-methyl-1H-imidazol-2-yl)methylidene]amino]propyl)benzenesulfonamide
-
-
4-(ethylamino)-6-(3-methoxypropyl)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
-
4-([(1E)-[4-(dimethylamino)phenyl]methylidene]amino)benzenesulfonamide
-
-
4-([[(1Z)-(2-chlorophenyl)methylidene]amino]methyl)benzenesulfonamide
-
-
4-([[(diethyl-l5-azanylidyne)methyl]disulfanyl]amino)benzenesulfonamide
-
-
4-amino-N-(4-sulfamoylcyclopenta-1,3-dien-1-yl)benzene-1-sulfonamide
-
4-aminosalicylic acid
-
noncompetitive inhibition of isozymes carbonic anhydrase I and II
4-S-isobutylamino-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
binds 800 times more strongly to carbonic anhydrase II than to carbonic anhydrase I
4-sulfosalicylic acid
-
uncompetitive inhibition of isozyme carbonic anhydrase I and competitive inhibition of isozyme carbonic anhydrase II
4-[(2R)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
-
4-[(2S)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
-
4-[(3,4,5-trihydroxytetrahydro-2H-pyran-2-yl)amino]benzenesulfonamide
-
4-[([(1Z)-[4-(dimethylamino)phenyl]methylidene]amino)methyl]benzenesulfonamide
-
-
4-[([[(diethyl-l5-azanylidyne)methyl]disulfanyl]amino)methyl]benzenesulfonamide
-
-
4-[2-[(7-methoxy-2-oxo-2H-chromen-4-yl)acetyl]hydrazino]benzenesulfonamide
-
-
4-[3-([(1E)-[4-(dimethylamino)phenyl]methylidene]amino)propyl]benzenesulfonamide
-
-
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-alpha-D-mannopyranosyl)-1H-1,2,3-triazole
-
-
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosyl)-1H-1,2,3-triazole
-
-
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
-
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-alpha-D-arabinopyranosyl)-1H-1,2,3-triazole
-
-
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
-
-
4-[4-(aminosulfonyl)phenyl]-1-(2',3',5'-tri-O-benzoyl-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
-
4-[4-(aminosulfonyl)phenyl]-1-(2'-acetamido-2'-deoxy'-3',4',6'-tri-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
-
4-[4-(aminosulfonyl)phenyl]-1-(2'-acetamido-2'-deoxy-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
-
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
-
-
4-[4-(aminosulfonyl)phenyl]-1-(hepta-O-acetyl-beta-D-maltopyranosyl)-1H-1,2,3-triazole
-
-
4-[N'-(1,1-dioxopyrido[4,3-e]-1,4,2-dithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
-
4-[N'-(6-chloro-7-cyano-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
-
4-[N'-(6-chloro-7-methyl-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
-
4-[[(1Z)-(1-bromonaphthalen-2-yl)methylidene]amino]benzenesulfonamide
-
-
4-[[(2R,3R)-3,4,5-trihydroxy-6-methyltetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
-
4-[[(2R,5S)-3,4,5-trihydroxy-6-methyltetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
-
4-[[(3R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
-
4-[[(3R,4R)-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
-
4-[[(4R)-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
-
4-[[(5R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
-
4-[[3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
-
5,5,5-tribromo-1,2,3,7,8,9,9a,11,16,17a-decahydro-5H-5lambda5-dipyrrolo[2,1-c:1',2'-f][1,4,6,9,5]benzotetraazastibacycloundecine-10,17-dione
5,6-diamino-1,3-dimethyluracil
inhibition of isozyme hCA I; inhibition of isozyme hCA II
5-(3alpha,12alpha-dihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
5-(3alpha,12alpha-dihydroxy-5beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
5-(3alpha,7alpha,12alpha-triacetoxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
5-(3alpha,7alpha,12alpha-triacetoxy-5beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
5-(3alpha,7alpha,12alpha-trihydroxy-5-beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
5-(3alpha,7alpha,12alpha-trihydroxy-5beta-cholanamido)-1,3,4-thiadiazole-2-sulfonamide
-
-
5-(hydroxymethyl)pyrimidine-2,4(1H,3H)-dione
inhibition of isozyme hCA I
5-([(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino)-1,3,4-thiadiazole-2-sulfonamide
-
-
5-bromo-1-(4-methylbenzene-1-sulfonyl)pyrimidine-2,4(1H,3H)-dione
inhibition of isozyme hCA I; inhibition of isozyme hCA II
5-bromo-1-(methanesulfonyl)pyrimidine-2,4(1H,3H)-dione
inhibition of isozyme hCA I; inhibition of isozyme hCA II
5-chlorosalicylic acid
-
uncompetitive inhibition of isozymes carbonic anhydrase I and II
5-sulfosalicylic acid
-
competitive inhibition of isozyme carbonic anhydrase I and noncompetitive inhibition of isozyme carbonic anhydrase II
5-[(benzylsulfonyl)(2,4-dichlorobenzyl)amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
5-[(benzylsulfonyl)(3,4,5-trimethoxybenzyl)amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
5-[cis-5-norbornene-endo-3-carboxy-2-carboxamido]-1,3,4-thiadiazole-2-sulfonamide
-
-
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
5-[[(pentafluorophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
5-[[(phenylcarbamoyl)carbamothioyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{(2,4-dichlorobenzyl)[(4-methylphenyl)sulfonyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{(4-bromobenzyl)[(4-methylphenyl)sulfonyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{(4-chlorobenzyl)[(4-methylphenyl)sulfonyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{(4-fluorobenzyl)[(4-methylphenyl)sulfonyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{(4-methoxybenzyl)[(4-methylphenyl)sulfonyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{(4-methylbenzyl)[(4-methylphenyl)sulfonyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{(benzylsulfonyl)[2-(4-bromophenyl)ethyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
5-{[(4-methylphenyl)sulfonyl](2-methylpropyl)amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{[(4-methylphenyl)sulfonyl](2-phenylethyl)amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{[(4-methylphenyl)sulfonyl](3,4,5-trimethoxybenzyl)amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{[(4-methylphenyl)sulfonyl](propan-2-yl)amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{[2-(4-bromophenyl)ethyl][(4-methylphenyl)sulfonyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
5-{[3-(2-methoxyphenyl)propyl][(4-methylphenyl)sulfonyl]amino}-1,3,4-thiadiazole-2-sulfonamide
-
-
6,6,6-trichloro-11-oxo-8,9,10,10a,11,12-hexahydro-6H-6lambda5-pyrimido[1,2-c]pyrrolo[2,1-g][1,3,5,2]triazastibepin-5-ium
6-amino-1,3-dimethyluracil
inhibition of isozyme hCA I; inhibition of isozyme hCA II
6-chloro-1,1-dioxo-1,2,3,4-tetrahydro-1lambda~6~,2,4-benzothiadiazine-7-sulfonamide
-
-
6-chloro-6,6-dimethyl-12-oxo-6,8,9,10,11,11a,12,13-octahydro-6lambda5-pyrido[2,1-g]pyrimido[1,2-c][1,3,5,2]triazastibepin-5-ium
7-hydroxy-1-methoxy-3-methyl-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
-
7-hydroxy-3-(hydroxymethyl)-1-methoxy-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
-
acetaldehyde
-
modification of carbonic anhydrase II with acetaldehyde leads to decreased enzyme activity, acetaldehyde (100 mM) in the presence of NaBH3(CN) causes 23.7% reduction in CA II activity, in the absence of NaBH3(CN) the activity is only slightly reduced
Acetylsalicylic acid
-
noncompetitive inhibition of isozymes carbonic anhydrase I and II
Benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate
-
benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate
-
benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate
-
benzyl (2E)-3-(3-hydroperoxy-4-hydroxyphenyl)prop-2-enoate
-
Chlorthalidone
chlorthalidone is a medium potency CA I, II, and IV inhibitor, a very effective inhibitor of CA VB, CA VII, CA IX, CA XII, and CA XIII and an ineffective inhibitor of isozymes CA III, VA, VI, and XIV
Co3+
-
competitive, strong inhibition of carbonic anhydrase esterase activity
Cu-GGHSLN
time-dependent inactivation of carbonic anhydrase I activity, within 3 h carbonic anhydrase I activity is eliminated at 0.005 mM Cu-GGHSLN
-
dibenzyl N',N'''-(tribromo-lambda5-stibanediyl)biscarbamimidothioate
36.0% inhibition of CO2 hydration reaction after 30 min
ethyl 3,4-dihydro-4-hydroxy-2H-thieno[3,2-e]-1,2-thiazine-3-carboxylate 1,1-dioxide
-
-
ethyl 3-(3-dimethylaminopropyl)-carbodiimide
Halalkalibacterium halodurans
80% inhibition at 5 mM, via irreversible modification of carboxyl groups or thepresence of catalytically active tyrosine in the enzyme molecule
hydrogencarbonate
good inhibitor of the Co(II)-substituted enzyme
indapamide
indapamide is a quite ineffective inhibitor of isozymes CA I, II, III, VA, VI, and XIV, a medium potency CA IV and CA VB inhibitor, and a very effective inhibitor of isozymes CA VII, IX, XII, and XIII
Isoorotic acid
inhibition of isozyme hCA I; inhibition of isozyme hCA II
methyl N-[(2,3,4,6-Tetra-O-acetyl-beta-D-glucosyl)sulfonyl]-L-4'-sulfamoylprolinate
-
methyl N-[(2,3,4,6-tetra-O-acetyl-beta-D-glucosyl)sulfonyl]-L-sulfamoylserinate
-
methyl-3-(3-phenylpropanoyl)-2,3-dihydro-2-thioxobenzo[d]oxazole-5-carboxylate
-
-
N'',N'''-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]carbonic dihydrazide
-
N'',N'''-bis[(E)-(2,4,6-trihydroxyphenyl)methylidene]carbonic dihydrazide
-
N'',N'''-bis[(E)-(2-hydroxy-3-methoxyphenyl)methylidene]carbonic dihydrazide
-
N'',N'''-bis[(E)-(2-hydroxy-5-methoxyphenyl)methylidene]carbonic dihydrazide
-
N'',N'''-bis[(E)-(3-ethoxy-2-hydroxyphenyl)methylidene]carbonic dihydrazide
-
N'',N'''-bis[(E)-(5-bromo-2-hydroxyphenyl)methylidene]carbonic dihydrazide
-
N-(1,1-dimethylethyl)-2-(3-methoxyphenyl)-3-[(2-propylaminol)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
N-(1,1-dimethylethyl)-2-(3-methoxyphenyl)-3-[(4-morpholinyl)methyl]-2H-thieno[3,2-e]-1,2-thiazine 1,1-dioxide
-
-
N-(1,1-dimethylethyl)-2-[4-(4-morpholinyl)-2-butenyl]-2H-thieno[3,2-e-]-1,2-thiazine-6-sulfonamide 1,1-dioxide
-
-
N-(1-(2-hydroxyphenylamino)-3-methyl-1-oxobutan-2-ylcarbamothioyl)benzamide
i.e. NK-154, binding structure, overview; i.e. NK-154, binding structure, overview; i.e. NK-154, binding structure, overview
N-(1-(2-hydroxyphenylamino)-4-methyl-1-oxopentan-2-ylcarbamothioyl) benzamide
i.e. NK-168, binding structure, overview; i.e. NK-168, binding structure, overview; i.e. NK-168, binding structure, overview
N-2'-sulfamoylethyl-S-(2,3,4,6-tetra-O-acetyl-1-thio-beta-D-glucopyranosyl)sulfonamide
-
N-3'-R-sulfamoylpyrrolidinyl-S-(1-thio-beta-D-glucopyranosyl)sulfonamide
-
N-3'-R-sulfamoylpyrrolidinyl-S-(2,3,4,6-tetra-O-acetyl-1-thio-beta-D-glucopyranosyl)sulfonamide
-
N-3'-sulfamoylpropyl-S-(2,3,4,6-tetra-O-acetyl-1-thio-beta-D-glucopyranosyl)sulfonamide
-
N-4'-sulfamoylpiperidinyl-S-(2,3,4,6-tetra-O-acetyl-1-thio-beta-D-glucopyranosyl)sulfonamide
-
N-5'-sulfamoylpentyl-S-(2,3,4,6-tetra-O-acetyl-1-thio-beta-D-glucopyranosyl)sulfonamide
-
N-hydroxysulfamide
isoenzyme hCA I; isoenzyme hCA IX; isoenzyme hCA XII; the inhibitor coordinates to the active site zinc ion by the ionized primary amino group, participating in an extended network of hydrogen bonds with amino acid residues Thr199, Thr200 and two water molecules, isoenzyme hCA II
N-[(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]sulfamic amide
-
-
N-[(4-[[(4-sulfamoylphenyl)carbamothioyl]amino]phenyl)sulfonyl]acetamide
-
-
N-[2,4-disulfamoyl-5-(trifluoromethyl)phenyl]-2-(7-methoxy-2-oxo-2H-chromen-4-yl)acetamide
-
-
N-[2,4-disulfamoyl-5-(trifluoromethyl)phenyl]-2-oxo-2H-chromene-3-carboxamide
-
-
N-[4-[(aminooxy)sulfinyl]phenyl]-4-[(diphenylcarbamoyl)amino]benzenesulfonamide
-
-
N-[5-[(aminooxy)sulfinyl]-1,3,4-thiadiazol-2-yl]-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
-
-
N-[[3-(1,3-dioxolan-2-yl)thien-2-yl]sulfonyl]-N-(1-methylethyl)-glycine ethyl ester
-
-
N-[[3-(1,3-dioxolan-2-yl)thien-2-yl]sulfonyl]-N-(2-propenyl)-glycine ethyl ester
-
-
N-[[3-(1,3-dioxolan-2-yl)thien-2-yl]sulfonyl]-N-(3-methoxyethyl)-glycine ethyl ester
-
-
N-[[3-(1,3-dioxolan-2-yl)thien-2-yl]sulfonyl]-N-methylcyclopropyl-glycine ethyl ester
-
-
N-[[3-(1,3-dioxolan-2-yl)thien-2-yl]sulfonyl]-N-[(3,4-dimethoxyphenyl)methyl]-glycine ethyl ester
-
-
N-[[3-(1,3-dioxolan-2-yl)thien-2-yl]sulfonyl]-N-[(3-methoxyphenyl)methyl]-glycine ethyl ester
-
-
N-[[3-(1,3-dioxolan-2-yl)thien-2-yl]sulfonyl]-N-[(4-methoxyphenyl)methyl]-glycine ethyl ester
-
-
N-[[3-(1,3-dioxolan-2-yl)thien-2-yl]sulfonyl]-N-[4-(morpholin-4-yl)phenyl]-glycine methyl ester
-
-
N-[[5-(aminosulfonyl)-2-formyl-thiophen-3-yl]sulfonyl]-N-methyl-glycine ethyl ester
-
-
Orotic acid
inhibition of isozyme hCA I; inhibition of isozyme hCA II
phosphate
binding structure analysis, overview. Phosphate binds to the catalytic zinc cofactor, each unit cell is comprised of four dimers of CrCAH3
sulfasalazine
-
noncompetitive inhibition of isozymes carbonic anhydrase I and II
Sulfonamides
-
affinity of carbonic anhydrase IV for sulfonamides is decreased up to 65fold compared to carbonic anhydrase II
tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate
-
tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate
-
tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate
-
trifluoromethanesulfonamide
U-shaped pH-dependence of the Gibbs energy of binding, the affinity is greatest in the near neutral pH region and diminished towards both the acidic and alkaline regions
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-2H,3aH,7H-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
(2Z)-2-(2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(3-bromobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(3-bromobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(3-methoxybenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(3-methoxybenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(4-chlorobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(4-chlorobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(4-methylpentan-2-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(4-methylpentan-2-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(5-bromo-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-(5-bromo-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-benzylidene-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(2Z)-2-benzylidene-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
-
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
-
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
-
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
-
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
-
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
-
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
-
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
-
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
-
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
-
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
-
1,1'-(tribromo-lambda5-stibanediyl)bis(2-aminopyridin-1-ium)
29.9% inhibition of CO2 hydration reaction after 30 min
1,1'-(tribromo-lambda5-stibanediyl)bis(2-aminopyridin-1-ium)
31.6% inhibition of CO2 hydration reaction after 30 min
1,1'-(tribromo-lambda5-stibanediyl)bis(2-aminopyrimidin-1-ium)
57.6% inhibition of CO2 hydration reaction after 30 min
1,1'-(tribromo-lambda5-stibanediyl)bis(2-aminopyrimidin-1-ium)
16.3% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-amino-4,6-dimethoxy-5-sulfanylpyrimidin-1-ium)
99.3% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-amino-4,6-dimethoxy-5-sulfanylpyrimidin-1-ium)
64.8% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-aminopyridin-1-ium)
49.2% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-aminopyridin-1-ium)
9.4% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-aminopyrimidin-1-ium)
98.4% inhibition of CO2 hydration reaction after 30 min
1,1'-(trichloro-lambda5-stibanediyl)bis(2-aminopyrimidin-1-ium)
90.2% inhibition of CO2 hydration reaction after 30 min
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
-
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
-
-
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
-
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
-
-
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
-
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
-
-
12,12,12-tribromo-7-oxo-6,7a,8,9,10,12-hexahydro-7H-12lambda5-pyrrolo[1',2':1,7][1,3,5,2]triazastibepino[4,3-b][1,3]benzothiazol-13-ium
92.3% inhibition of CO2 hydration reaction after 30 min
12,12,12-tribromo-7-oxo-6,7a,8,9,10,12-hexahydro-7H-12lambda5-pyrrolo[1',2':1,7][1,3,5,2]triazastibepino[4,3-b][1,3]benzothiazol-13-ium
11.1% inhibition of CO2 hydration reaction after 30 min; 18.4% inhibition of CO2 hydration reaction after 30 min
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
-
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
-
-
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
-
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
-
-
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hpalphaCA; isoenzyme hpbetaCA
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA XII; isoenzyme hCA XIV
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme gammaCA
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV catalytic domain
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
efficient inhibitor of only isozymes CA I and II
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme mCA XIII
2-(hydroxymethyl)-4-nitro-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
-
2-(hydroxymethyl)-4-nitro-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
-
2-methoxy-N-[(1-methylpyrrolidin-2-yl)methyl]-5-sulfamoylbenzamide
-
2-methoxy-N-[(1-methylpyrrolidin-2-yl)methyl]-5-sulfamoylbenzamide
-
-
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme mCA XIII
2-[[(5-chlorothiophen-2-yl)(hydroxy)methyl]amino]-1-(trichloro[2-[2-(5-chlorothiophen-2-yl)-2-oxoethyl]pyrimidin-1-ium-1-yl]-lambda5-stibanyl)pyrimidin-1-ium
18.7% inhibition of CO2 hydration reaction after 30 min
2-[[(5-chlorothiophen-2-yl)(hydroxy)methyl]amino]-1-(trichloro[2-[2-(5-chlorothiophen-2-yl)-2-oxoethyl]pyrimidin-1-ium-1-yl]-lambda5-stibanyl)pyrimidin-1-ium
62.5% inhibition of CO2 hydration reaction after 30 min
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hpalphaCA, i.e. daranide; isoenzyme hpbetaCA, i.e. daranide
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA I, i.e. daranide; isoenzyme hCA II, i.e. daranide; isoenzyme hCA III, i.e. daranide; isoenzyme hCA IV, i.e. daranide; isoenzyme hCA IX, i.e. daranide; isoenzyme hCA VA, i.e. daranide; isoenzyme hCA VB, i.e. daranide; isoenzyme hCA VI, i.e. daranide; isoenzyme hCA VII, i.e. daranide; isoenzyme hCA XII, i.e. daranide; isoenzyme hCA XIV, i.e. daranide
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme gammaCA, i.e. daranide
4,5-dichloro-benzene-1,3-disulfonamide
-
shows effective carbonic anhydrase inhibitory activity
4-(aminosulfonyl)-N-[2-[4-(aminosulfonyl)phenyl]ethyl]benzamide
-
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
-
4-[(acetyloxy)amino]-N-[4-(aminosulfonyl)phenyl]benzenesulfonamide
-
4-[(anilinocarbonyl)amino]-6-chlorobenzene-1,3-disulfonamide
-
4-[2-[(anilinocarbonothioyl)amino]ethyl]benzenesulfonamide
-
4-[2-[([[4-(aminosulfonyl)phenyl]amino]carbonothioyl)amino]ethyl]benzenesulfonamide
-
4-[2-[([[4-(aminosulfonyl)phenyl]amino]carbonothioyl)amino]ethyl]benzenesulfonamide
-
-
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
-
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
-
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
-
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
-
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
-
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
-
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
-
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
-
-
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
-
-
4-[[(anilinocarbonothioyl)amino]methyl]benzenesulfonamide
-
5,5,5-tribromo-1,2,3,7,8,9,9a,11,16,17a-decahydro-5H-5lambda5-dipyrrolo[2,1-c:1',2'-f][1,4,6,9,5]benzotetraazastibacycloundecine-10,17-dione
83.9% inhibition of CO2 hydration reaction after 30 min
5,5,5-tribromo-1,2,3,7,8,9,9a,11,16,17a-decahydro-5H-5lambda5-dipyrrolo[2,1-c:1',2'-f][1,4,6,9,5]benzotetraazastibacycloundecine-10,17-dione
9.9% inhibition of CO2 hydration reaction after 30 min
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
-
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
-
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
-
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
5-[[(4-bromophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
5-[[(4-nitrophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
6,6,6-trichloro-11-oxo-8,9,10,10a,11,12-hexahydro-6H-6lambda5-pyrimido[1,2-c]pyrrolo[2,1-g][1,3,5,2]triazastibepin-5-ium
31.0% inhibition of CO2 hydration reaction after 30 min
6,6,6-trichloro-11-oxo-8,9,10,10a,11,12-hexahydro-6H-6lambda5-pyrimido[1,2-c]pyrrolo[2,1-g][1,3,5,2]triazastibepin-5-ium
25.1% inhibition of CO2 hydration reaction after 30 min
6-chloro-1,1-dioxo-1,2,3,4-tetrahydro-1lambda6,2,4-benzothiadiazine-7-sulfonamide
-
6-chloro-1,1-dioxo-1,2,3,4-tetrahydro-1lambda6,2,4-benzothiadiazine-7-sulfonamide
-
-
6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide
-
-
6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide
-
-
6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide
-
-
6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide
-
-
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hpalphaCA; isoenzyme hpbetaCA
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme gammaCA
6-chloro-6,6-dimethyl-12-oxo-6,8,9,10,11,11a,12,13-octahydro-6lambda5-pyrido[2,1-g]pyrimido[1,2-c][1,3,5,2]triazastibepin-5-ium
99.3% inhibition of CO2 hydration reaction after 30 min
6-chloro-6,6-dimethyl-12-oxo-6,8,9,10,11,11a,12,13-octahydro-6lambda5-pyrido[2,1-g]pyrimido[1,2-c][1,3,5,2]triazastibepin-5-ium
22.9% inhibition of CO2 hydration reaction after 30 min
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hpalphaCA; isoenzyme hpbetaCA
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA III; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA XII; isoenzyme hCA XIV
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme gammaCA
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme mCA XIII
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hpalphaCA; isoenzyme hpbetaCA
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme gammaCA
acetazolamide
-
at 0.5 mM inhibition of the cabonic anhydrase activity of the high molecular mass protein and stimulation of activity of the low molecular mass carrier in the PSII-membranes. At 0.5 mM acetazolamide moderately inhibits the carbonic anhydrase activity of PSI membranes
acetazolamide
-
100 mM, the firmly-membrane-associated activity is less sensitive to inhibition than the loosely-membrane associated enzyme
acetazolamide
binding structure analysis, overview. Each unit cell is comprised of four dimers of CrCAH3
acetazolamide
-
at very low CO2 concentrations enzyme inhibition reduces photosynthesis
acetazolamide
Elephas trogontherii
-
cytosolic isoenzyme; inner peripheral isoenzyme; integral isoenzyme; outer peripheral isoenzyme
acetazolamide
-
carbonic anhydrase A is 100times less sensitive than carbonic anhydrase C; carbonic anhydrase A is completely inhibited at 1 mM, carbonic anhydrase C is completely inhibited at 0.01 mM
acetazolamide
-
-
acetazolamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV
acetazolamide
AAZ, a sulfonamide inhibitor; AAZ, a sulfonamide inhibitor; AAZ, a sulfonamide inhibitor
acetazolamide
i.e. 5-acetamido-1,3,4-thiadiazole-2-sulfonamide; i.e. 5-acetamido-1,3,4-thiadiazole-2-sulfonamide; i.e. 5-acetamido-1,3,4-thiadiazole-2-sulfonamide
acetazolamide
the recombinant MgaCA shows a very similar acetazolamide inhibition features when compared to those of the native enzyme (MgaCA)
acetazolamide
-
increases carbonic anhydrase activity of photosystem 2 membranes at concentrations lower than 0.001 mM and suppresses this activity only at higher concentrations. Carbonic anhydrase activity of photosystem 1 membranes is suppressed
acetazolamide
-
shows effective carbonic anhydrase inhibitory activity
acetazolamide
highly inhibited by acetazolamide, i.e. 5-acetamido-1,3,4-thiadiazole-2-sulfonamide
acetazolamide
-
at very low CO2 concentrations enzyme inhibition reduces photosynthesis
Ag+
-
competitive, strong inhibition of carbonic anhydrase esterase activity
Al3+
-
competitive, very strong inhibition of carbonic anhydrase esterase activity
benzolamide
-
shows effective carbonic anhydrase inhibitory activity
brinzolamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV catalytic domain
brinzolamide
-
shows effective carbonic anhydrase inhibitory activity
Carbonate
weak inhibitor of the Zn(II)-substituted enzyme, best inhibitor of the Co(II)-substituted enzyme
Cl-
-
100 mM, the firmly-membrane-associated activity is less sensitive to inhibition than the loosely-membrane associated enzyme
CN-
best anion inhibitors for Zn2+-substituted enzyme are cyanate and hydrogen sulfide
Cu2+
-
competitive, very strong inhibition of carbonic anhydrase esterase activity
Cu2+
Halalkalibacterium halodurans
inhibits completely at 5 mM, 66% inhibition at 1 mM
dextran-bound acetazolamide
-
at very low CO2 concentrations enzyme inhibition reduces photosynthesis. Inhibition of enzyme reduces growth by about 10% at pH 8.4
-
dextran-bound acetazolamide
-
at very low CO2 concentrations enzyme inhibition reduces photosynthesis
-
dibenzyl N',N'''-(trichloro-lambda5-stibanediyl)biscarbamimidothioate
26.7% inhibition of CO2 hydration reaction after 30 min
dibenzyl N',N'''-(trichloro-lambda5-stibanediyl)biscarbamimidothioate
54.4% inhibition of CO2 hydration reaction after 30 min
dorzolamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV catalytic domain
dorzolamide
-
shows effective carbonic anhydrase inhibitory activity
DTT
50% inhibition at 0.5 mM, complete inhibition at above 2.5 mM
EMD 486019
EMD 486019 acts as a strong inhibitor of isozymes carbonic anhydrase II, VB, VII, IX, XII, and XIV
ethanol
-
carbonic anhydrase activity is significantly inhibited by 2ml/kg ethanol for up to 3 h following intraperitoneally administration
ethoxyzolamide
-
effectively suppresses the carbonic anhydrase activity of photosystem 2 membranes. Carbonic anhydrase activity of PS1 membranes is suppressed alike by both inhibitors
ethoxzolamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV
ethoxzolamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV catalytic domain
ethoxzolamide
strong binding, U-shaped pH-dependence of the Gibbs energy of binding, the affinity is greatest in the near neutral pH region and diminished towards both the acidic and alkaline regions
ethoxzolamide
-
shows effective carbonic anhydrase inhibitory activity
Fe2+
Halalkalibacterium halodurans
inhibits completely at 5 mM, 74% inhibition at 1 mM
Fe3+
Halalkalibacterium halodurans
inhibits completely at 5 mM, 75% inhibition at 1 mM
Furosemide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV
H2NSO2NH2
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA IX; isoenzyme hCA XII
H2NSO3H
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA IX; isoenzyme hCA XII
Hg2+
-
competitive, strong inhibition of carbonic anhydrase esterase activity
Hg2+
Halalkalibacterium halodurans
inhibits completely at 5 mM, 78% inhibition at 1 mM
HS-
best anion inhibitors for Zn2+-substituted enzyme are cyanate and hydrogen sulfide
hydrochlorothiazide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV
hydrogen sulfide
best inhibitor of the Zn(II)-substituted enzyme
hydrogen sulfite
weak inhibitor of the Zn(II)-substituted enzyme
I-
-
100 mM, the firmly-membrane-associated activity is less sensitive to inhibition than the loosely-membrane associated enzyme
KSCN
-
uncompetitive inhibition of outer peripheral, cytosolic, inner peripheral and integral isoenzyme
KSCN
Elephas trogontherii
-
cytosolic isoenzyme; inner peripheral isoenzyme; integral isoenzyme; outer peripheral isoenzyme
methazolamide
-
shows effective carbonic anhydrase inhibitory activity
N'',N'''-bis[(E)-(2,6-dichlorophenyl)methylidene]carbonic dihydrazide
mixed-type inhibition
N'',N'''-bis[(E)-(2-chloro-5-nitrophenyl)methylidene]carbonic dihydrazide
-
N'',N'''-bis[(E)-(2-chloro-5-nitrophenyl)methylidene]carbonic dihydrazide
mixed-type inhibition
N'',N'''-bis[(E)-(2-chlorophenyl)methylidene]carbonic dihydrazide
mixed-type inhibition
N'',N'''-bis[(E)-(2-nitrophenyl)methylidene]carbonic dihydrazide
mixed-type inhibition
N'',N'''-bis[(E)-(4-bromophenyl)methylidene]carbonic dihydrazide
mixed-type inhibition
N'',N'''-bis[(E)-(4-nitrophenyl)methylidene]carbonic dihydrazide
mixed-type inhibition
N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)furan-2-carboxamide
-
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
-
-
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
-
-
N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
-
-
N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
-
-
N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
-
-
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hpalphaCA; isoenzyme hpbetaCA
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA III; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA XII; isoenzyme hCA XIV
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme gammaCA
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme mCA XIII
NaN3
-
uncompetitive inhibition of outer peripheral, cytosolic, inner peripheral and integral isoenzyme
NaN3
Elephas trogontherii
-
cytosolic isoenzyme; inner peripheral isoenzyme; integral isoenzyme; outer peripheral isoenzyme
Ni2+
Halalkalibacterium halodurans
inhibits by 84% at 5 mM, 80% inhibition at 1 mM
nitrate
mutants M3 and M4 are more resistent against inhibition by nitrate compared to wild-type and mutants M1 and M2
Pb2+
-
competitive, moderate inhibition of carbonic anhydrase esterase activity
salicylic acid
-
noncompetitive inhibition of isozymes carbonic anhydrase I and II
SDS
the wild-type enzyme is inactivated at 0.4% w/v, the mutant enzymes are more stable showing residual activity at that concentration
sulfanilamide
-
uncompetitive inhibition of outer peripheral, cytosolic, inner peripheral and integral isoenzyme
sulthiame
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XIV
thiocyanate
weak inhibitor of the Zn(II)-substituted enzyme
topiramate
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV
Zn2+
-
competitive, strong inhibition of carbonic anhydrase esterase activity
Zn2+
-
the enzyme binds three catalytic Zn2+ ions at symmetry-related subunit interfaces. Zinc binding drives the folding and association of the homotrimeric enzyme
zonisamide
isoenzyme hCA I; isoenzyme hCA II; isoenzyme hCA III; isoenzyme hCA IV; isoenzyme hCA IX; isoenzyme hCA VA; isoenzyme hCA VB; isoenzyme hCA VI; isoenzyme hCA VII; isoenzyme hCA XII; isoenzyme hCA XIV catalytic domain
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
-
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
-
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
-
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
-
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
-
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
-
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
-
-
additional information
-
dianionic inhibitors depress the rate of H+ transfer during turnover by stabilizing the protonated from of Lys64
-
additional information
carbohydrazones as another class of carbonic anhydrase inhibitors, synthesis, kinetics, and ligand docking studies, overview. Single crystal X-ray diffraction, structural coordinates of bovine carbonic anhydrase (PDB ID 1V9E) is used for docking of carbohydrazone compounds, three-dimensional structure analysis. No inhibition by N'',N'''-bis[(E)-(4-chlorophenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-fluorophenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-phenylmethylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-hydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(3-hydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(4-hydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2,3-dihydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2,5-dihydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(5-bromo-2-hydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2,4,6-trihydroxyphenyl)methylidene]carbonicdihydrazide, N'',N'''-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(3-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(4-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-hydroxy-5-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(2-hydroxy-3-methoxyphenyl)methylidene]carbonic dihydrazide, N'',N'''-bis[(E)-(3-ethoxy-2-hydroxyphenyl)methylidene]carbonic dihydrazide, and N'',N'''-bis[(E)-(3,4-dimethoxyphenyl)methylidene]carbonic dihydrazide
-
additional information
antimony(III) complexes inhibit alpha-carbonic anhydrase isozyme II from bovine erythrocytes. No inhibition by 5
-
additional information
best bsCA II inhibitors are some glycosylated sulfanilamides, aliphatic sulfamates, and halogenated sulfanilamides
-
additional information
-
best bsCA II inhibitors are some glycosylated sulfanilamides, aliphatic sulfamates, and halogenated sulfanilamides
-
additional information
-
perchlorate is not an inhibitor in concentrations up to 200 mM
-
additional information
perchlorate, tetrafluoroborate, azide, fluoride, and bromide are not inhibitory for the enzyme
-
additional information
-
perchlorate, tetrafluoroborate, azide, fluoride, and bromide are not inhibitory for the enzyme
-
additional information
-
the inhibitory metals might be dangerous at low micromolar concentrations for fish carbonic anhydrase enzymes
-
additional information
-
sulfate, sulfide, azide, nitrate, nitrite and iodide exhibit strong inhibitory activity in the micromolar range (Ki values of 5.5-15.5 mM). Cyanide, bromide, chloride, and carbonate are moderate inhibitors, whereas other anions show only weak activities. The anions inhibit enzyme HmCA in a similar manner to other alpha-CAs from mammals, but the susceptibility to various anions differs significantly between the Halomonas sp. and other organism CAs, overview
-
additional information
no inhibition of HCA II by citrate and no conformational changes of amino-acid side chains as a result of the use of citrate at pH 6.0-11.0
-
additional information
-
no inhibition of HCA II by citrate and no conformational changes of amino-acid side chains as a result of the use of citrate at pH 6.0-11.0
-
additional information
-
synthesis of two series of disubstituted coumarins incorporating ether and acetyl/propionyl moieties in positions 6,7 and 7,8 of the heterocyclic ring. The compounds are very weak or ineffective as inhibitors of the housekeeping, offtarget isozymes CA I and CA II. The 6,7-disubstituted series show ineffective inhibition also for the transmembrane tumor-associated isoforms CA IX and XII, whereas the corresponding isomeric 7,8-disubstituted coumarins show nanomolar/subnanomolar inhibition of CA IX/XII, overview. No inhibition by 12 and 13
-
additional information
-
N-beta-glycosyl sulfamides are selective inhibitors of the cancer-associated carbonic anhydrase isoforms IX and XII
-
additional information
-
development and synthesis of a series of compounds incorporating regioisomeric phenylethynylbenzenesulfonamide moieties, analysis of potential as inhibitors of the four human isozymes, hCA I, hCA II, hCA IX, and hCA XII. The position of the sulfamoyl group with respect to the alkyne functionality, and the nature of the moieties substituting the second aromatic ring are the principal structural features influencing CA inhibition. The para-sulfamoyl-substituted derivatives are effective inhibitors of CA IX and XII, the meta-substituted regioisomers of CA I, X and XII, whereas the ortho-substituted sulfonamides ae weak inhibitors of CA I, II and IX, but inhibit ignificantly CA XII, structure-activity relationship study, overview
-
additional information
-
carbonic anhydrases are inhibited by sulfonamides, inorganic anions, phenols, coumarins (acting as prodrugs) and polyamines. Development of hydroxy-, methoxy-substituted benzoic acids as well as di-, tri-methoxy benzenes as submicromolar-low micromolar inhibitors of carbonic anhydrase isozymes, molecular docking and inhibition mechanism, overview
-
additional information
-
synthesis of 2-[(p-toluenesulfonamido)-N-yl]-l,3,4-thiadiazole-5-sulfonamide inhibitors, inhibitory potencies versus isozymes CAII, docking study, overview
-
additional information
-
an additional 3-fluoro substituent on the 4-amino-benzenesulfonamide scaffold of inhibitors alters the inhibition profiles against the cytosolic isozymes hCA I, II, III, VII and XIII, interaction analysis, overview. The binding differences render the inhibitors more isozyme-specific. Docking studies, overview
-
additional information
-
some natural phenols show effective hCA II inhibitory effects, in the same range as the clinically used sulfonamide acetazolamide, and might be used as leads for generating enzyme inhibitors possibly targeting other CA isozymes
-
additional information
presence of D2O reduces catalysis, but does not change how it proceeds; presence of D2O reduces catalysis, but does not change how it proceeds
-
additional information
presence of D2O reduces catalysis, but does not change how it proceeds; presence of D2O reduces catalysis, but does not change how it proceeds
-
additional information
-
presence of D2O reduces catalysis, but does not change how it proceeds; presence of D2O reduces catalysis, but does not change how it proceeds
-
additional information
structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, in silico modeling of inhibitors in CA I, oveview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview
-
additional information
structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, in silico modeling of inhibitors in CA I, oveview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview
-
additional information
structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, in silico modeling of inhibitors in CA I, oveview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview
-
additional information
structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, in silico modeling of inhibitors in CA I, oveview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview; structure-activity relationships of benzenesulfonamide-based inhibitors towards carbonic anhydrase isoform specificity, inhibition of different human isozymes, overview
-
additional information
2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview
-
additional information
2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview
-
additional information
2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview
-
additional information
2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview
-
additional information
-
2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview; 2-benzylpiperazine is a scaffold for potent human carbonic anhydrase inhibitors, compounds synthesis, enzyme inhibition, and enantioselectivity, overview
-
additional information
isozyme hCA II is inhibited by flavonoids, poor inhibition by pelargonin; isozyme hCA I is inhibited by flavonoids, poor inhibition by pelargonin
-
additional information
isozyme hCA II is inhibited by flavonoids, poor inhibition by pelargonin; isozyme hCA I is inhibited by flavonoids, poor inhibition by pelargonin
-
additional information
-
isozyme hCA II is inhibited by flavonoids, poor inhibition by pelargonin; isozyme hCA I is inhibited by flavonoids, poor inhibition by pelargonin
-
additional information
3-[[(3,4-dimethoxyphenyl)methyl]amino]-2,5,6-trifluoro-4-(2-hydroxyethanesulfonyl)benzene-1-sulfonamide does not exhibit selectivity for CA XIV
-
additional information
-
3-[[(3,4-dimethoxyphenyl)methyl]amino]-2,5,6-trifluoro-4-(2-hydroxyethanesulfonyl)benzene-1-sulfonamide does not exhibit selectivity for CA XIV
-
additional information
inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 2FW4, modeling; inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 3IAI, modeling. No inhibition by pyrogallol; inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 5AML, modeling
-
additional information
inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 2FW4, modeling; inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 3IAI, modeling. No inhibition by pyrogallol; inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 5AML, modeling
-
additional information
inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 2FW4, modeling; inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 3IAI, modeling. No inhibition by pyrogallol; inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 5AML, modeling
-
additional information
-
inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 2FW4, modeling; inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 3IAI, modeling. No inhibition by pyrogallol; inhibitor synthesis and isozyme in silico docking study using enzyme structure, PDB ID 5AML, modeling
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additional information
benzothiazole derivative inhibitor synthesis, overview; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate
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additional information
benzothiazole derivative inhibitor synthesis, overview; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate
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additional information
benzothiazole derivative inhibitor synthesis, overview; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate
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additional information
benzothiazole derivative inhibitor synthesis, overview; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate
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additional information
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benzothiazole derivative inhibitor synthesis, overview; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; benzothiazole derivative inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate; inhibitor synthesis, overview. No inhibition by benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, (S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate, (S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate, tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate, (S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate, (S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate, and (S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate
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additional information
some uracil derivatives have carbonic anhydrase inhibitory properties, overview; some uracil derivatives have carbonic anhydrase inhibitory properties, overview
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additional information
some uracil derivatives have carbonic anhydrase inhibitory properties, overview; some uracil derivatives have carbonic anhydrase inhibitory properties, overview
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additional information
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some uracil derivatives have carbonic anhydrase inhibitory properties, overview; some uracil derivatives have carbonic anhydrase inhibitory properties, overview
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additional information
synthesis, X-ray structure, in silico calculation, and carbonic anhydrase inhibitory properties of benzylimidazole metal complexes, i.e. three coordination compounds of formula [M(bmim)2Cl2], crystal structures of metal complexes, overview. Each complex incorporates 1-benzyl-2-methylimidazole (bmim) as ligand. The coordination polyhedron around the metal center for all complexes has a quasi-regular tetragonal geometry. In the 1-benzyl-2-methylimidazole ligand, imidazole moiety is connected to phenyl cycle via a methylene linker. Density functional theory calculations are carried out on the title compounds, with Co2+, Zn2+, and Hg2+, and as well on hypothetical complexes (with Cu2+, Ni2+) in order to elucidate their electronic and molecular structure. All three complxes do not inhibit the enzyme significantly; synthesis, X-ray structure, in silico calculation, and carbonic anhydrase inhibitory properties of benzylimidazole metal complexes, i.e. three coordination compounds of formula [M(bmim)2Cl2], crystal structures of metal complexes, overview. Each complex incorporates 1-benzyl-2-methylimidazole (bmim) as ligand. The coordination polyhedron around the metal center for all complexes has a quasi-regular tetragonal geometry. In the 1-benzyl-2-methylimidazole ligand, imidazole moiety is connected to phenyl cycle via a methylene linker. Density functional theory calculations are carried out on the title compounds, with Co2+, Zn2+, and Hg2+, and as well on hypothetical complexes (with Cu2+, Ni2+) in order to elucidate their electronic and molecular structure. Only compound [Hg(bmim)2Cl2] exhibits a modest inhibitory effect against enzyme hCA I, probably due to the affinity of Hg(II) for His residues at the entrance of the active site cavity
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additional information
synthesis, X-ray structure, in silico calculation, and carbonic anhydrase inhibitory properties of benzylimidazole metal complexes, i.e. three coordination compounds of formula [M(bmim)2Cl2], crystal structures of metal complexes, overview. Each complex incorporates 1-benzyl-2-methylimidazole (bmim) as ligand. The coordination polyhedron around the metal center for all complexes has a quasi-regular tetragonal geometry. In the 1-benzyl-2-methylimidazole ligand, imidazole moiety is connected to phenyl cycle via a methylene linker. Density functional theory calculations are carried out on the title compounds, with Co2+, Zn2+, and Hg2+, and as well on hypothetical complexes (with Cu2+, Ni2+) in order to elucidate their electronic and molecular structure. All three complxes do not inhibit the enzyme significantly; synthesis, X-ray structure, in silico calculation, and carbonic anhydrase inhibitory properties of benzylimidazole metal complexes, i.e. three coordination compounds of formula [M(bmim)2Cl2], crystal structures of metal complexes, overview. Each complex incorporates 1-benzyl-2-methylimidazole (bmim) as ligand. The coordination polyhedron around the metal center for all complexes has a quasi-regular tetragonal geometry. In the 1-benzyl-2-methylimidazole ligand, imidazole moiety is connected to phenyl cycle via a methylene linker. Density functional theory calculations are carried out on the title compounds, with Co2+, Zn2+, and Hg2+, and as well on hypothetical complexes (with Cu2+, Ni2+) in order to elucidate their electronic and molecular structure. Only compound [Hg(bmim)2Cl2] exhibits a modest inhibitory effect against enzyme hCA I, probably due to the affinity of Hg(II) for His residues at the entrance of the active site cavity
-
additional information
development and synthesis of a class of CA IX inhibitors that comprise a sulfamate as the zinc binding group, a variable linker, and a carbohydrate tail moiety
-
additional information
-
fluoride, chloride, and sulfate do not inhibit the Zn2+-substituted enzyme and the Co2+-substituted enzyme appreciably; Zn(II)- and Co(II)-substituted enzymes show a very different behavior against anion inhibitors.The best Zn-Cam anion inhibitors are hydrogen sulfide and cyanate whereas thiocyanate, azide, carbonate, nitrite, and hydrogensulfite are weaker inhibitors. The inhibition of the Zn(II)-substituted enzyme by sulfide is puzzling since Cam is proposed to be located outside the cytoplasmic membrane where it is exposed to high levels of sulfide in the anaerobic environments. The best inhibitors of the Co(II)-substituted enzyme is carbonate, followed by nitrate and hydrogencarbonate. Fluoride, chloride, and sulfate do not inhibit either Zn(II)- or Co(II)-substituted enzyme appreciably up to concentrations of 200 mM. This lack of inhibition may represent an adaptation to marine environments high in chloride and sulfate
-
additional information
fluoride, chloride, and sulfate do not inhibit the Zn2+-substituted enzyme and the Co2+-substituted enzyme appreciably; Zn(II)- and Co(II)-substituted enzymes show a very different behavior against anion inhibitors.The best Zn-Cam anion inhibitors are hydrogen sulfide and cyanate whereas thiocyanate, azide, carbonate, nitrite, and hydrogensulfite are weaker inhibitors. The inhibition of the Zn(II)-substituted enzyme by sulfide is puzzling since Cam is proposed to be located outside the cytoplasmic membrane where it is exposed to high levels of sulfide in the anaerobic environments. The best inhibitors of the Co(II)-substituted enzyme is carbonate, followed by nitrate and hydrogencarbonate. Fluoride, chloride, and sulfate do not inhibit either Zn(II)- or Co(II)-substituted enzyme appreciably up to concentrations of 200 mM. This lack of inhibition may represent an adaptation to marine environments high in chloride and sulfate
-
additional information
-
fluoride, chloride, and sulfate do not inhibit the enzyme appreciably
-
additional information
inhibitor molecular docking simulations using the three-dimensional structure of the thiocyanate-bound Mtb Rv1248 enzyme, PDB ID 1YLK, binding structures, overview; inhibitor molecular docking simulations using the three-dimensional structure of the thiocyanate-bound Mtb Rv3588c enzyme, PDB ID 2A5V, binding structures, overview
-
additional information
-
inhibitor molecular docking simulations using the three-dimensional structure of the thiocyanate-bound Mtb Rv1248 enzyme, PDB ID 1YLK, binding structures, overview; inhibitor molecular docking simulations using the three-dimensional structure of the thiocyanate-bound Mtb Rv3588c enzyme, PDB ID 2A5V, binding structures, overview
-
additional information
-
fluoride, sulfate, perchlorate and tetrafluoroborate do not inhibit appreciably NcoCA, whereas the other halides, pseudohalides, bicarbonate, nitrate, nitrite and many complex inorganic anions cause inhibition in the millimolar range
-
additional information
-
the epipodites and antennal gland display decreased levels of mRNA expression and stable enzyme activity at 24 h after hypo-osmotic stress
-
additional information
antimony(III) complexes inhibit glutathione reductase activity of chloroplast, and a number of them also exhibit good inhibitory efficiency against the photosynthetic and carbonic anhydrase activity of Pisum sativum photosystem II
-
additional information
-
not inhibited by quinine, qinghausu, and chloroquine
-
additional information
sulfonamides CA inhibitors generally show much weaker inhibitory activity against PfCAdom compared to truncated PfCA
-
additional information
-
sulfonamides CA inhibitors generally show much weaker inhibitory activity against PfCAdom compared to truncated PfCA
-
additional information
no inhibition by fluoride, iodide, chloride, azide, sulfate, P2O74-, V2O74-, ReO4-, chlorate, tetrafluoroborate, PF6-, and CF3SO3-
-
additional information
-
bromide, iodide and sulfamide, are the best anion inhibitors, with Ki values of 0.0087-0.0108 mM. Benzenesulfonamides substituted in 2-, 4- and 3,4-positions with amino, alkyl, halogeno and hydroxyalkyl moieties have Ki values in the range of 0.000976-0.01845 mM. Better inhibition with Ki values in the range of 154-654 nM is observed for benzenesulfonamides incorporating aminoalkyl/carboxyalkyl moieties or halogenosulfanilamides, benzene-1,3-disulfonamides, simple heterocyclic sulfonamides and sulfanilyl-sulfonamides. The clinically used sulfonamides/sulfamates, e.g. acetazolamide, ethoxzolamide, methazolamide, dorzolamide, topiramate, celecoxib, generally show effective scCA inhibitory activity, with Ki values in the range of 82.6-133 nM, overview
-
additional information
-
strongest inhibitors of enzyme CA are aromatic or heteroaromatic sulfonamides
-
additional information
Synechocystis sp. PCC 6803 / Kazusa
the C-terminal tail appears to partly inhibit activity, possibly indicating a role in minimizing the activity of unencapsulated enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-(naphthalen-2-ylsulfonyl)propanehydrazide hydrochloride
-
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[(4-iodophenyl)sulfonyl]propanehydrazide hydrochloride
submicromolar activator of isoform CA II, but shows much higher affinities for isoforms CA I and IX
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[(4-methoxyphenyl)sulfonyl]propanehydrazide hydrochloride
-
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[(4-methylphenyl)sulfonyl]propanehydrazide hydrochloride
effective CA IX activator
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[(4-nitrophenyl)sulfonyl]propanehydrazide hydrochloride
effective CA IX activator
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[(pentafluorophenyl)sulfonyl]propanehydrazide hydrochloride
-
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[[4-(trifluoromethyl)phenyl]sulfonyl]propanehydrazide hydrochloride
-
(2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide hydrochloride
-
(2S)-2-amino-N'-[(4-bromophenyl)sulfonyl]-3-(1H-imidazol-4-yl)propanehydrazide hydrochloride
effective CA IX activator
(2S)-2-amino-N'-[(4-chlorophenyl)sulfonyl]-3-(1H-imidazol-4-yl)propanehydrazide hydrochloride
-
(2S)-2-amino-N'-[(4-cyanophenyl)sulfonyl]-3-(1H-imidazol-4-yl)propanehydrazide hydrochloride
-
(2S)-2-amino-N'-[(4-fluorophenyl)sulfonyl]-3-(1H-imidazol-4-yl)propanehydrazide hydrochloride
effective CA IX activator
(2S)-2-amino-N'-[(4-tert-butylphenyl)sulfonyl]-3-(1H-imidazol-4-yl)propanehydrazide hydrochloride
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,3,4,6-tetramethylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,4,6-trimethylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,4-dimethyl-6-phenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-di-iso-propyl-4-methylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-di-iso-propyl-4-phenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-di-n-butyl-4-methylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-di-n-butyl-4-phenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-di-n-propyl-4-methylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-di-n-propyl-4-phenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-diethyl-4-methylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-diethyl-4-phenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-dimethyl-3,5-(nonane-1,9-diyl)pyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-dimethyl-4-phenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2,6-diphenyl-4-methylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2-ethyl-4,6-dimethylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2-ethyl-4,6-diphenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2-iso-propyl-4,6-dimethylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2-iso-propyl-4,6-diphenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2-methyl-4,6-diphenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2-n-butyl -4,6 -dimethylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2-n-butyl-4,6-diphenylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2-n-propyl-4,6-dimethylpyridinium hexafluorophosphate
-
-
1-[2-(1H-imidazol-4-yl)-ethyl]-2-n-propyl-4,6-diphenylpyridinium hexafluorophosphate
-
-
2-mercaptoethanol
-
increases the activity of isozyme CAH7 by 69% but has no effect on the activity of isozyme CAH8
4-[2-(4-dimethylaminophenyl)-vinyl]-1-[2-(1H-imidazol-4-yl)ethyl]-2,6-di-isopropylpyridinium hexafluorophosphate
-
-
acetazolamide
-
increases carbonic anhydrase activity of photosystem 2 membranes at concentrations lower than 0.001 mM and suppresses this activity only at higher concentrations. Carbonic anhydrase activity of photosystem 1 membranes is suppressed
aminoethyl-piperazine/morpholine
-
carbonic anhydrase III is efficiently activated by aminoethyl-piperazine/morpholine
-
CAA12i
carbonic anhydrase activator 12i, enzyme binding structure determination and analysis, the location of the imidazole moiety in both conformations of CAA12i flips between two small hydrophobic cavities flanking Phe131. This movement may be analogous to the movement observed with His64 as it performs its proton-shuttling function. Conformation A may represent the in conformation of His64, as this position forms an extension of the proton wire network. In conformation B, the CAA12i tail moiety is extended away from the proton network, and this may be analogous to the out conformation of His64. Overall, the crystal structure of this CAA12i ligand indicates possible transient motion that may be essential to its activation function
H2O2
the enzyme loses activity when it was exposed to 3% H2O2
imidazole
addition of 50 mM imidazole to the assay buffer increases the kcat of the enzyme more than 4fold
Phosphorus
-
increases the growth rate of the cells and the enzyme activity
timolol
-
the formal name is (2S)-1-[(1,1-dimethylethyl)amino]-3-[[4-(4-morpholinyl)-1,2,5-thiadiazol-3-yl]oxy]-2-propanol, timolol noncompetitively activates carbonic anhydrases I and II activities, timolol increases the value of Vmax but does not influence the value of Km
1-(2-aminoethyl)-piperazine
-
effectively activates Zn-gamma-class carbonic anhydrase
2-pyridylmethylamine
-
effectively activates Zn-gamma-class carbonic anhydrase
4-(2-aminoethyl)-morpholine
-
carbonic anhydrase IV is efficiently activated by 4-(2-aminoethyl)-morpholine
4-amino-L-phenylalanine
-
carbonic anhydrase IV is efficiently activated by 4-amino-L-phenylalanine
D-Phe
-
effective beta-class carbonic anhydrase activator
L-Tyr
-
effective beta-class carbonic anhydrase activator
serotonin
-
carbonic anhydrases III and IV are efficiently activated by serotinin
additional information
-
activating effects on the cytosolic isozymes hCA I, hCA II, and hCA VII, competitive steady-state activation kinetics of the pyridinium histamine derivatives, KA values, overview
-
additional information
-
Ka values of activators of isozymes hCA I and hCA II, overview
-
additional information
addition of the PG domain of iszyme CA IX to the catalytic CA-domain increases the catalytic activity by about 63%
-
additional information
-
addition of the PG domain of iszyme CA IX to the catalytic CA-domain increases the catalytic activity by about 63%
-
additional information
proposed mechanism of CA enzyme activation by the compounds
-
additional information
-
proposed mechanism of CA enzyme activation by the compounds
-
additional information
lack of proximal tubule CIC-5 is associated with CAIII induction
-
additional information
-
the external carbonic anhydrase is activated by hydration, especially at low pH, the increase is modest (1.6fold) and transitory, if the pH of the hydration medium is set at 8. Relatively high internal carbonic anhydrase activity is present in the dry colonies, at pH 6, no appreciable variation is observed during subsequent dehydration, whereas, at pH 8.0, dehydration induces a recovery of the intracellular carbonic anhydrase activity, the presence of light does not affect internal carbonic anhydrase activity during dehydration at either pH
-
additional information
-
carbonic anhydrase mRNA and enzyme activity are significantly increased in shrimp gills at 24 h after hypo-osmotic stress
-
additional information
-
L-adrenaline and some piperazines incorporating aminoethyl moieties were the most effective scCA activators
-
additional information
the carbonic anhydrase gene is expressed 2fold more during the dark than the light
-
additional information
-
the carbonic anhydrase gene is expressed 2fold more during the dark than the light
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.935
4-nitrophenyl phosphate
-
isoform carbonic anhydrase I, at pH 7.4 and 25°C
2.195
4-nitrophenyl phosphate
-
isoform carbonic anhydrase II, at pH 7.4 and 25°C
0.012
CO2
-
isoform CA II, in the presence of 4.5 mM timolol, at 25°C in 0.01 M HEPES buffer (pH 7.4)
0.013
CO2
-
isoform CA II, in the presence of 2.0 mM timolol, at 25°C in 0.01 M HEPES buffer (pH 7.4)
0.02
CO2
-
isoform CA I, in the presence of 1.5 or 3.0 mM timolol, at 25°C in 0.01 M HEPES buffer (pH 7.4)
0.31
CO2
-
pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H200T
2.8
CO2
-
pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N62V
3.1
CO2
pH 7.5, 25°C, enzyme cultured with supplemental zinc
3.9
CO2
-
pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant T200H
5.8
CO2
-
pH 8.5, 25°C, mutant D34A/R36A, imidazole buffer
6.09
CO2
pH 7.5, 37°C, variant R59H, 100 mM guanidine hydrochloride
6.6
CO2
-
pH 8.75, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H67N
7
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the absence of Zn2+
7.1
CO2
-
pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62N
7.3
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Co2+
7.3
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Mg2+
7.3
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Mn2+
7.3
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of Zn2+
7.5
CO2
-
pH 7.23, 1-methylimidazolebuffer, carbonic anhydrase I mutant V62N,H67N,H200T
7.5
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Zn2+
7.5
CO2
recombinant extracellular domain of CA IX expressed in Sf9 cells, in the absence of Zn2+
9.3
CO2
-
native isozyme carbonic anhydrase II, in 10 mM HEPES, 0.1 M Na2SO4, pH 7.5
9.4
CO2
-
pH 8.72, 1,2-dimethyimidazole buffer, carbonic anhydrase I mutant V62N,H67N
10
CO2
-
pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H200T
12.2
CO2
pH 7.5, 37°C, variant R59A, 100 mM methylguanidine
12.8
CO2
pH 7.5, 37°C, variant R59A, 100 mM 1.3-diaminoguanidine
13
CO2
-
isoform CA II, at 25°C in 0.01 M HEPES buffer pH 7.4, in the absence of timolol
14
CO2
-
pH 8.75, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62N,H67N,H200T
14
CO2
-
pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N67HV
15.3
CO2
-
pH 8.5, 25°C, mutant D34A, imidazole buffer
16.3
CO2
pH 7.5, 37°C, variant R59K, 100 mM guanidine hydrochloride
17.3
CO2
pH 7.5, 37°C, variant R59C, 100 mM methylguanidine, variant R59Q, 100 mM guanidine hydrochloride
19
CO2
-
isoform CA I, at 25°C in 0.01 M HEPES buffer pH 7.4, in the absence of timolol
19.1
CO2
pH 7.5, 37°C, variant R59K, 100 mM guanidine hydrochloride
19.3
CO2
pH 7.5, 37°C, variant R59E, 100 mM guanidine hydrochloride
21.8
CO2
pH 7.5, 37°C, wild-type, without guanidine hydrochloride
25
CO2
pH 7.5, 37°C, variant R59H, without guanidine hydrochloride
33.4
CO2
pH 7.5, 37°C, variant R59K, without guanidine hydrochloride
33.9
CO2
pH 7.5, 37°C, variant R59Q, without guanidine hydrochloride
43.3
CO2
pH 7.5, 37°C, variant R59M, without guanidine hydrochloride
47.1
CO2
-
pH 8.5, 25°C, mutant R36A, imidazole buffer
51.4
CO2
pH 7.5, 37°C, variant R59E, without guanidine hydrochloride
6.5
H2CO3
carbonate dehydratase activity, recombinant enzyme, pH and temperature not specified in the publication
21.5
H2CO3
-
pH not specified in the publication, 4°C, assay using the delta pH method
additional information
additional information
kinetics
-
additional information
additional information
-
influence of pH and buffer composition on Km-values
-
additional information
additional information
-
influence of pH-value and buffer composition on Km-value on native enzyme and on an activated derivative with modified thiol groups
-
additional information
additional information
-
influence of buffer composition and pH on the Km-value
-
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
-
steady-state kinetics, overview
-
additional information
additional information
-
kinetics of the esterase activity with 4-nitrophenylacetate as substrate
-
additional information
additional information
-
Km is 4.0 mM with 4-nitrophenyl acetate, pH 9.0, 30°C, esterase activity
-
additional information
additional information
-
steady-state kinetic analysis of the Co2+-substituted enzyme, overview
-
additional information
additional information
-
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
during the second catalytic stage, the zinc-bound 18O-labeled hydroxide is protonated, forming H2 18O, which is then released into solution, 18O-exchange kinetic analysis, overview
-
additional information
additional information
Caminibacter sp.
-
intrinsic second order kinetic constant kcat/KM for the CO2 hydration reaction catalyzed by the immobilized CA
-
additional information
additional information
kinetic and thermodynamic analysis, molecular modelling, overview
-
additional information
additional information
-
kinetic and thermodynamic analysis, molecular modelling, overview
-
additional information
additional information
-
kinetics of 4-nitrophenyl acetate hydrolysis reaction
-
additional information
additional information
kinetics of free and immobilized enzymes with esterase activity on substrate 4-nitrophenyl acetate
-
additional information
additional information
-
kinetics, stopped-flow assay method
-
additional information
additional information
Salmo trutta Labrax Coruhensis
-
Lineweaver-Burk kinetic plots
-
additional information
additional information
steady-state kinetics and isotope effects of recombinant enzyme variants, overview
-
additional information
additional information
steady-state kinetics and isotope effects of recombinant enzyme variants, overview
-
additional information
additional information
-
steady-state kinetics and isotope effects of recombinant enzyme variants, overview
-
additional information
additional information
stopped flow CO2 hydrase assay method
-
additional information
additional information
Synechocystis sp. PCC 6803 / Kazusa
stopped-flow spectrophotometric kinetic analysis
-
additional information
additional information
stopped-flow spectrophotometric kinetic analysis
-
additional information
additional information
stopped-flow spectrophotometric measurements
-
additional information
additional information
-
stopped-flow spectrophotometric measurements
-
additional information
additional information
stopped-flow technique, kinetic analysis
-
additional information
additional information
-
stopped-flow technique, kinetic analysis
-
additional information
additional information
the recombinant MgaCA shows a very similar kinetic features when compared to those of the native enzyme (MgaCA)
-
additional information
additional information
-
the recombinant MgaCA shows a very similar kinetic features when compared to those of the native enzyme (MgaCA)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000493
CO2
pH 7.5, 25°C, enzyme cultured with supplemental zinc
0.0052
CO2
pH 7.5, 25°C, enzyme cultured with supplemental iron
10
CO2
pH 7.5, 37°C, variant R59Q, without guanidine hydrochloride
12
CO2
pH 7.5, 37°C, variant R59A, 100 mM 1.3-diaminoguanidine, variant R59H plus 100 mM guanidine hydrochloride
13
CO2
pH 7.5, 37°C, variant R59M, without guanidine hydrochloride
42
CO2
pH 7.5, 37°C, variant R59H, without guanidine hydrochloride
67
CO2
pH 7.5, 37°C, variant R59E, without guanidine hydrochloride
150
CO2
-
pH 7.9, temperature not specified in the publication, the activities depended on culture conditions, ranging between 20/sec and 150/sec
159
CO2
pH 7.5, 37°C, variant R59M, 100 mM guanidine hydrochloride
200
CO2
-
pH 7.9, temperature not specified in the publication, the activities depended on culture conditions, ranging between 80/sec and 200/sec
627
CO2
pH 7.5, 37°C, variant R59Q, 100 mM guanidine hydrochloride
1180
CO2
-
pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N and carbonic anhydrase I mutant H67N
1500
CO2
-
pH 8.5, 25°C, mutant D34A/R36A, imidazole buffer
2000
CO2
-
pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62N
2740
CO2
pH 7.5, 37°C, variant R59K, 100 mM guanidine hydrochloride
2830
CO2
-
pH 8.75, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H67N
3340
CO2
Synechocystis sp. PCC 6803 / Kazusa
recombinant full-length CcaA274 enzyme, pH 7.5, 25°C, CO2 hydration reaction
3500
CO2
-
pH 8.72, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62B, H67B
3670
CO2
-
pH 7.23, 1-methylimidazolebuffer, carbonic anhydrase I mutant V62N,H67N,H200T
4000
CO2
-
pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant T200H
4720
CO2
pH 7.5, 37°C, variant R59K, without guanidine hydrochloride
5500
CO2
-
pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H200T
5690
CO2
pH 7.5, 37°C, variant R59A, 100 mM methylguanidine
8170
CO2
-
pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N62V
8500
CO2
-
pH 8.75, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62N,H67N,H200T
9100
CO2
-
pH 8.5, 25°C, mutant D34A, imidazole buffer
11000
CO2
isozyme bsCAII, pH 8.3, temperature not specified in the publication
13700
CO2
Synechocystis sp. PCC 6803 / Kazusa
recombinant full-length CcaA274 enzyme, pH 9.5, 25°C, CO2 hydration reaction
20000
CO2
pH 7.5, 37°C, variant R59E, without guanidine hydrochloride
22900
CO2
pH 7.5, 37°C, wild-type, 100 mM guanidine hydrochloride
28300
CO2
-
pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N67H
31000
CO2
Synechocystis sp. PCC 6803 / Kazusa
recombinant truncated CcaA220 enzyme, pH 9.5, 25°C, CO2 hydration reaction
62900
CO2
pH 7.5, 37°C, wild-type, without guanidine hydrochloride
64000
CO2
isozyme bsCAI, pH 8.3, temperature not specified in the publication
130000
CO2
measured with hydration of CO2 activity assay, pH 7.5-8.3, 0°C
140000
CO2
pH 7.5, 22°C, truncated form PfCA1, CO2 hydration reaction
380000
CO2
pH 7.5, 22°C, long enzyme form PfCAdom, CO2 hydration reaction
390000
CO2
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
390000
CO2
-
Can2, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
420000
CO2
CO2 hydration, pH 8.3, 22°C, recombinant enzyme
450000
CO2
-
truncated form of carbonic anhydrase VII lacking the amino-terminal 23 residues of recombinant enzyme
680000
CO2
-
Can2, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine
800000
CO2
-
CaNce103, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
940000
CO2
-
pH not specified in the publication, temperature not specified in the publication
1100000
CO2
recombinant extracellular domain of CA IX expressed in Sf9 cells, in the absence of Zn2+
1400000
CO2
-
native isozyme carbonic anhydrase II, in 10 mM HEPES, 0.1 M Na2SO4, pH 7.5
2010000
CO2
-
CaNce103, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine
3800000
CO2
recombinant CA IX catalytic domain expressed in Escherichia coli
3800000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the absence of Zn2+
4200000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Zn2+
11000000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Mg2+
12000000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Co2+
25000000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Mn2+
25000000
CO2
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of Zn2+
13000
H2CO3
-
pH not specified in the publication, 4°C, assay using the delta pH method
68000
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and aerobically purified
231000
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Methanosarcina acetivorans and anaerobically purified
243000
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and anaerobically purified
890000
H2CO3
carbonate dehydratase activity, recombinant enzyme, pH and temperature not specified in the publication
1070000
histamine
-
at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine
additional information
additional information
-
influence of buffer composition and pH on the turnover-number
-
additional information
additional information
-
influence of pH-value and buffer composition and the native enzyme and on an activated derivative with modified thiol groups
-
additional information
additional information
-
20.3/s with 4-nitrophenyl acetate, pH 9.0, 30°C, esterase activity
-
additional information
additional information
-
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
-
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
additional information
additional information
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
additional information
additional information
-
first order kinetic constant at 25°C is 9160000 L/(mol s)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00016
CO2
pH 7.5, 25°C, enzyme cultured with supplemental zinc
0.0017
CO2
pH 7.5, 25°C, enzyme cultured with supplemental iron
1190
CO2
Synechocystis sp. PCC 6803 / Kazusa
recombinant full-length CcaA274 enzyme, pH 7.5, 25°C, CO2 hydration reaction
3900
CO2
isozyme bsCAI, pH 8.3, temperature not specified in the publication
5400
CO2
pH 7.5, 22°C, truncated form PfCA1, CO2 hydration reaction
8900
CO2
isozyme bsCAII, pH 8.3, temperature not specified in the publication
17300
CO2
Synechocystis sp. PCC 6803 / Kazusa
full-length CcaA274 enzyme, pH 9.5, 25°C, CO2 hydration reaction
33000
CO2
measured with hydration of CO2 activity assay, pH 7.5-8.3, 0°C
35000
CO2
CO2 hydration, pH 8.3, 22°C, recombinant enzyme
37000
CO2
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
72000
CO2
pH 7.5, 22°C, long enzyme form PfCAdom, CO2 hydration reaction
98000
CO2
-
pH not specified in the publication, temperature not specified in the publication
120000
CO2
pH 7.6, temperature not specified in the publication, wild-type
130000
CO2
pH 7.6, temperature not specified in the publication, mutant A23C/L203C/C206S
3100
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and aerobically purified
3900
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Methanosarcina acetivorans and anaerobically purified
5400
H2CO3
-
pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and anaerobically purified
130000
H2CO3
carbonate dehydratase activity, recombinant enzyme, pH and temperature not specified in the publication
additional information
additional information
-
Km/kcat values for 4-nitrophenylacetate hydrolysis by wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
kinetic constants of apoenzyme reconstituted with Zn2+, Co2+, Cu2+, Mn2+, Ni2+, Cd2+, or Fe2+
-
additional information
additional information
-
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
additional information
additional information
the Fe2+-reconstituted enzyme produced in Escherichia coli and purified anaerobically contains iron with effective kcat and kcat/Km values exceeding the values for Zn2+-reconstituted enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00334 - 0.35
(2E)-2-[(4-hydroxy-3-methylphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
0.00383 - 0.00803
(2E)-2-[(4-hydroxyphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
0.000095 - 0.239
(2R)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
0.000102 - 0.231
(2S)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
0.000079 - 0.000144
(2Z)-2-(2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
0.0000134 - 0.0000431
(2Z)-2-(3-bromobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
0.0000345 - 0.0000401
(2Z)-2-(3-methoxybenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
0.0000184 - 0.0000953
(2Z)-2-(4-chlorobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
0.0000331
(2Z)-2-(4-fluorobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000195 - 0.0000524
(2Z)-2-(4-methylpentan-2-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
0.0000725 - 0.000152
(2Z)-2-(5-bromo-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
0.0000211 - 0.0000279
(2Z)-2-benzylidene-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
0.0000038 - 0.00025
(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl sulfamate
0.00026 - 0.007835
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-1,1-dioxo-1,2,3,4-tetrahydro-1lambda~6~-thieno[3,2-e][1,2]thiazine-6-sulfonamide
0.0000025 - 0.084
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
0.0000063 - 0.079
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
0.000963 - 0.00794
(4S,6S)-4-(ethylamino)-6-methyl-7,7-dioxo-4,5,6,7-tetrahydro-7lambda~6~-thieno[2,3-b]thiopyran-2-sulfonamide
0.00007 - 0.0105
(5Z)-2-amino-5-(4-hydroxy-3-methoxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
0.0000334 - 0.000205
(R)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
0.0000051 - 0.002626
(R)-17(R)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
0.000002 - 0.000232
(R)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
0.0000377
(R)-4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.000019 - 0.000181
(R)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
0.0000443
(R)-4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.0000023 - 0.000166
(R)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
0.0000026 - 0.00152
(R)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
0.0000036 - 0.001207
(R)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
0.0000062 - 0.00036
(R)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
0.0000078 - 0.000227
(S)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
4.1
(S)-2-(2-ammoniopropanamido)-4-methylbenzo[d]thiazol-3-ium di-2,2,2-trifluoroacetate
pH 7.5, 22°C
0.0000316 - 0.000186
(S)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
0.000707
(S)-4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.000006 - 0.0000797
(S)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
0.0000828
(S)-4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.0000054 - 0.000191
(S)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
0.000002 - 0.000139
(S)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
0.0000927 - 0.0005426
(S)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
0.0000078 - 0.0003303
(S)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
0.0000622 - 0.001589
(S)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
0.005 - 0.0711
(S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate
0.0726
(S)-benzyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate
pH 7.5, 22°C
0.0847
(S)-tert-butyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate
pH 7.5, 22°C
4.1
(S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate
pH 7.5, 22°C
0.086
(S)-tert-butyl (1-((4-methylbenzo[d]thiazol-2-yl)amino)-1-oxopropan-2-yl)carbamate
pH 7.5, 22°C
0.0454
(S)-tert-butyl (1-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate
pH 7.5, 22°C
0.000048 - 0.0089
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
0.00046 - 0.0044
1-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-4-(4-sulfamoylphenyl)-1H-1,2,3-triazole
0.003055
2,3,4,5,6-pentafluoro-N-(2-sulfamoylphenyl)benzenesulfonamide
-
-
0.003441
2,3,4,5,6-pentafluoro-N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)benzamide
-
-
0.006867
2,3,4,5,6-pentafluoro-N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]benzamide
-
-
0.0000009 - 45
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
0.0032 - 0.00726
2-(4-hydroxyphenyl)ethyl (2E)-3-(3-hydroperoxy-4-hydroxyphenyl)prop-2-enoate
0.001436
2-(7-methoxy-2-oxo-2H-chromen-4-yl)-N-(2-sulfamoylphenyl)acetamide
-
-
0.004578
2-(7-methoxy-2-oxo-2H-chromen-4-yl)-N-(3-sulfamoylphenyl)acetamide
-
-
0.00097
2-(7-methoxy-2-oxo-2H-chromen-4-yl)-N-(4-sulfamoylphenyl)acetamide
-
-
0.000893 - 0.0128
2-(hydroxymethyl)-4-nitro-N-[2-(4-sulfamoylphenyl)ethyl]benzene-1-sulfonamide
0.0000502 - 0.000134
2-(hydroxymethyl)-4-nitro-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
0.000091
2-amino-pyrimidin-4-yl-sulfanilamide
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.0674
2-bromobenzene-1-sulfonamide
-
pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity
0.01317
2-oxo-N-[2-(4-sulfamoylphenyl)ethyl]-2H-chromene-3-carboxamide
-
-
0.00395 - 0.00803
2-[3-[2-(3-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
0.0051 - 0.00713
2-[4-[2-(4-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
0.0000048 - 0.00083
3,4,6-tri-O-acetyl-2-deoxy-N-sulfamoyl-beta-D-arabino-hexopyranosylamine
0.000057 - 0.00051
3-(methylsulfanyl)-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
0.000009 - 0.00021
3-morpholin-4-yl-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
0.000069 - 0.368
4,4'-[(1R,2R,3S,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
0.000079 - 0.354
4,4'-[(1R,2S,3R,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
0.000016
4-(2-([(4-sulfamoylphenyl)carbamothioyl]amino)ethyl)benzenesulfonamide
-
pH 7.5, 20°C
0.000621
4-(2-[(phenylcarbamothioyl)amino]ethyl)benzenesulfonamide
-
pH 7.5, 20°C
0.025
4-(3-[[(1E)-(1-methyl-1H-imidazol-2-yl)methylidene]amino]propyl)benzenesulfonamide
-
-
0.000624
4-(4-sulfanilyl-aminoethyl)-benzenesulfonamide
-
at 20°C, pH 8.3
0.000971
4-(4-sulfanilyl-aminomethyl)-benzenesulfonamide
-
at 20°C, pH 8.3
0.025
4-([(1E)-[4-(dimethylamino)phenyl]methylidene]amino)benzenesulfonamide
-
-
0.000679
4-([(phenylcarbamothioyl)amino]methyl)benzenesulfonamide
-
pH 7.5, 20°C
0.00025
4-([[(1Z)-(2-chlorophenyl)methylidene]amino]methyl)benzenesulfonamide
-
-
0.002997
4-([[(diethyl-l5-azanylidyne)methyl]disulfanyl]amino)benzenesulfonamide
-
-
0.000968
4-amino-6-trifluoromethyl-benzene-1,3-disulfonamide
-
at 20°C, pH 8.3
0.0303
4-amino-N-(4,6-dimethylpyrimidin-2-yl)benzene-1-sulfonamide
-
pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity
0.0216
4-amino-N-(pyrimidin-2-yl)benzene-1-sulfonamide
-
pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity
0.09125
4-amino-N-carbamimidoylbenzene-1-sulfonamide
-
pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity
0.000079
4-chloro-6-[(phenylcarbamoyl)amino]benzene-1,3-disulfonamide
-
pH 7.5, 20°C
0.08275
4-chlorobenzene-1-sulfonamide
-
pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity
0.000815
4-methyl-5-imino-1,3,4-thiadiazoline-2-sulfonamide
-
at 20°C, pH 8.3
0.000067
4-[(3,4,5-trihydroxytetrahydro-2H-pyran-2-yl)amino]benzenesulfonamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.025
4-[([(1Z)-[4-(dimethylamino)phenyl]methylidene]amino)methyl]benzenesulfonamide
-
-
0.008392
4-[([[(diethyl-l5-azanylidyne)methyl]disulfanyl]amino)methyl]benzenesulfonamide
-
-
0.0000069
4-[2-(2-thienyl)acetamido]-3-chlorobenzenesulfonamide
-
isoform CA VII
0.004057
4-[2-[(2-oxo-2H-chromen-3-yl)carbonyl]hydrazino]benzenesulfonamide
-
-
0.003506
4-[2-[(7-methoxy-2-oxo-2H-chromen-4-yl)acetyl]hydrazino]benzenesulfonamide
-
-
0.000003 - 0.00303
4-[2-[([[4-(aminosulfonyl)phenyl]amino]carbonothioyl)amino]ethyl]benzenesulfonamide
0.025
4-[3-([(1E)-[4-(dimethylamino)phenyl]methylidene]amino)propyl]benzenesulfonamide
-
-
0.0000016 - 0.000005
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-alpha-D-mannopyranosyl)-1H-1,2,3-triazole
0.0000087 - 0.0043
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosyl)-1H-1,2,3-triazole
0.0000091 - 0.0044
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
0.0000082 - 0.000134
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-alpha-D-arabinopyranosyl)-1H-1,2,3-triazole
0.0000099 - 0.00013
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
0.0001 - 0.0053
4-[4-(aminosulfonyl)phenyl]-1-(2',3',5'-tri-O-benzoyl-beta-D-ribofuranosyl)-1H-1,2,3-triazole
0.000101 - 0.005
4-[4-(aminosulfonyl)phenyl]-1-(2'-acetamido-2'-deoxy'-3',4',6'-tri-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
0.000085
4-[4-(aminosulfonyl)phenyl]-1-(2'-acetamido-2'-deoxy-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000023 - 0.000028
4-[4-(aminosulfonyl)phenyl]-1-(alpha-D-arabinopyranosyl)-1H-1,2,3-triazole
0.0000028 - 0.0000076
4-[4-(aminosulfonyl)phenyl]-1-(alpha-D-mannopyranosyl)-1H-1,2,3-triazole
0.0000093 - 0.00012
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-galactopyranosyl)-1H-1,2,3-triazole
0.0000089 - 0.00038
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-glucopyranosyl)-1H-1,2,3-triazole
0.0000084 - 0.00056
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
0.00012 - 0.0025
4-[4-(aminosulfonyl)phenyl]-1-(hepta-O-acetyl-beta-D-maltopyranosyl)-1H-1,2,3-triazole
0.000021 - 0.0348
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
0.0000046 - 0.0089
4-[N'-(1,1-dioxopyrido[4,3-e]-1,4,2-dithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
0.0000034 - 0.0000923
4-[N'-(6-chloro-7-cyano-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
0.0000081
4-[N'-(6-chloro-7-methyl-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000058 - 0.000101
4-[N'-(6-chloro-7-methyl-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazyno]-3-pyridinesulfonamide
0.004162
4-[[(1Z)-(1-bromonaphthalen-2-yl)methylidene]amino]benzenesulfonamide
-
-
0.000019
4-[[(2R,3R)-3,4,5-trihydroxy-6-methyltetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000028
4-[[(2R,5S)-3,4,5-trihydroxy-6-methyltetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000103
4-[[(3R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000065
4-[[(3R,4R)-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0000089
4-[[(4R)-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0000092
4-[[(5R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00011
4-[[3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]amino]benzenesulfonamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0000061
5-(2-phenylacetamido)-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA VII
0.000012
5-(formylamino)-1,3,4-thiadiazole-2-sulfonamide
-
wild-type, pH 7.5, 20°C
0.04951
5-(hydroxymethyl)pyrimidine-2,4(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.04185
5-([(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino)-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.0000019
5-([(4-bromophenyl)sulfonyl]amino)-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.0000035
5-([(4-nitrophenyl)sulfonyl]amino)-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.0000069
5-[2-(2-thienyl)acetamido]-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA VII
0.000186 - 0.0805
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
0.000186 - 0.000663
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
0.002583
5-[[(pentafluorophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
0.000315
5-[[(phenylcarbamoyl)carbamothioyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
-
0.0777
6-acetyl-7-adamantylethoxy-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0074
6-acetyl-7-ethoxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.00803
6-acetyl-7-hydroxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.00758
6-acetyl-7-propoxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0196 - 0.0683
6-chloro-1,1-dioxo-1,2,3,4-tetrahydro-1lambda6,2,4-benzothiadiazine-7-sulfonamide
0.000153
6-chloro-1,1-dioxo-1,2,3,4-tetrahydro-1lambda~6~,2,4-benzothiadiazine-7-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA38
-
0.0000502 - 0.000394
6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide
0.0000035 - 8
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
0.05776
6-methylpyrimidine-2,4(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.000093 - 0.201
7-hydroxy-1-methoxy-3-methyl-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
0.000094 - 0.374
7-hydroxy-3-(hydroxymethyl)-1-methoxy-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
0.008015
7-hydroxy-6-propanoyl-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0102 - 4.1
Benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate
0.0868
benzyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate
pH 7.5, 22°C
0.0675
benzyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate
pH 7.5, 22°C
0.00178
N'',N'''-bis[(E)-(2,6-dichlorophenyl)methylidene]carbonic dihydrazide
pH 7.4, 25°C
0.00358
N'',N'''-bis[(E)-(2-chloro-5-nitrophenyl)methylidene]carbonic dihydrazide
pH 7.4, 25°C
0.00412
N'',N'''-bis[(E)-(2-chlorophenyl)methylidene]carbonic dihydrazide
pH 7.4, 25°C
0.00181
N'',N'''-bis[(E)-(2-nitrophenyl)methylidene]carbonic dihydrazide
pH 7.4, 25°C
0.00252
N'',N'''-bis[(E)-(4-bromophenyl)methylidene]carbonic dihydrazide
pH 7.4, 25°C
0.00235
N'',N'''-bis[(E)-(4-nitrophenyl)methylidene]carbonic dihydrazide
pH 7.4, 25°C
0.000068 - 1
N-(1-(2-hydroxyphenylamino)-4-methyl-1-oxopentan-2-ylcarbamothioyl) benzamide
0.0000105
N-(5-(aminosulfonyl)-1,3,4-thiadiazol-2-yl)acetamide
-
at 20°C, pH 8.3
0.0011 - 0.03
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
0.0000036
N-[(2E)-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]furan-2-carboxamide
-
pH 7.5, 20°C
0.001875 - 0.00458
N-[(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]sulfamic amide
0.004622
N-[(4-[[(4-sulfamoylphenyl)carbamothioyl]amino]phenyl)sulfonyl]acetamide
-
-
0.002519
N-[2,4-disulfamoyl-5-(trifluoromethyl)phenyl]-2-(7-methoxy-2-oxo-2H-chromen-4-yl)acetamide
-
-
0.009034
N-[2,4-disulfamoyl-5-(trifluoromethyl)phenyl]-2-oxo-2H-chromene-3-carboxamide
-
-
0.01652
N-[4-[(aminooxy)sulfinyl]phenyl]-4-[(diphenylcarbamoyl)amino]benzenesulfonamide
-
-
0.000192
N-[5-[(aminooxy)sulfinyl]-1,3,4-thiadiazol-2-yl]-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
-
-
0.0081
phenyl-boronic acid
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
0.0066 - 0.0859
tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate
0.0888
tert-butyl (2-((4-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-carbamate
pH 7.5, 22°C
0.0084 - 0.0782
tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate
0.0007 - 0.0024
tert-butyl 5-[[(aminosulfonyl)amino]sulfonyl]-2-hydroperoxyphenylcarbamate
0.000295 - 0.0148
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-2H,3aH,7H-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
0.00001 - 0.1
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
0.00003 - 0.0012
[3-[(tert-butoxycarbonyl)amino]-4-hydroperoxyphenyl]sulfonylsulfamic acid
0.0004
(2,4,6-triisopropylphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0015
(2,4,6-triisopropylphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.003
(2,4,6-triisopropylphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0008
(2,4,6-tripropylphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0021
(2,4,6-tripropylphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.00334
(2E)-2-[(4-hydroxy-3-methylphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
pH 8.3, 22°C
0.021
(2E)-2-[(4-hydroxy-3-methylphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
pH 8.3, 22°C
0.35
(2E)-2-[(4-hydroxy-3-methylphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
pH 8.3, 22°C
0.00383
(2E)-2-[(4-hydroxyphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
pH 8.3, 22°C
0.00715
(2E)-2-[(4-hydroxyphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
pH 8.3, 22°C
0.00803
(2E)-2-[(4-hydroxyphenyl)methylidene]-N-(5-sulfanylidene-4,5-dihydro-1,3,4-thiadiazol-2-yl)hydrazine-1-carboxamide
pH 8.3, 22°C
0.00536
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid
pH 8.3, 25°C, recombinant enzyme
0.00592
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid
pH 8.3, 25°C, recombinant enzyme
0.0067
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid
pH 8.3, 25°C, recombinant enzyme
0.0024
(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid
pH 8.3, 25°C, recombinant enzyme
0.00564
(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid
pH 8.3, 25°C, recombinant enzyme
0.00713
(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoic acid
pH 8.3, 25°C, recombinant enzyme
0.000095
(2R)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
isoform CA VA
0.000114
(2R)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
isoform CA VB
0.0083
(2R)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
isoform CA II
0.239
(2R)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
isoform CA I
0.000102
(2S)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
isoform CA VB
0.000108
(2S)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
isoform CA VA
0.008
(2S)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
isoform CA II
0.231
(2S)-3-(3-chloro-4-hydroxyphenyl)-2-[[(2E)-4-methoxy-4-oxobut-2-enoyl]amino]propanoic acid
-
isoform CA I
0.000079
(2Z)-2-(2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.000144
(2Z)-2-(2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000134
(2Z)-2-(3-bromobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000431
(2Z)-2-(3-bromobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000345
(2Z)-2-(3-methoxybenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000401
(2Z)-2-(3-methoxybenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000184
(2Z)-2-(4-chlorobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000643
(2Z)-2-(4-chlorobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000947
(2Z)-2-(4-chlorobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000953
(2Z)-2-(4-chlorobenzylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000195
(2Z)-2-(4-methylpentan-2-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000524
(2Z)-2-(4-methylpentan-2-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000725
(2Z)-2-(5-bromo-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.000152
(2Z)-2-(5-bromo-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000211
(2Z)-2-benzylidene-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0000279
(2Z)-2-benzylidene-N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.0003
(3,5-dichloro-2-hydroxyphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0005
(3,5-dichloro-2-hydroxyphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0021
(3,5-dichloro-2-hydroxyphenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00009
(3-chloro-4-nitrophenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0003
(3-chloro-4-nitrophenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.002
(3-chloro-4-nitrophenyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0000038
(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl sulfamate
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.000005
(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl sulfamate
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.000058
(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl sulfamate
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.00025
(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl sulfamate
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.00026
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-1,1-dioxo-1,2,3,4-tetrahydro-1lambda~6~-thieno[3,2-e][1,2]thiazine-6-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA29
0.007835
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-1,1-dioxo-1,2,3,4-tetrahydro-1lambda~6~-thieno[3,2-e][1,2]thiazine-6-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0000025
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
pH 7.5, 20°C
0.0000873
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
pH 7.5, 20°C
0.000278
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
pH 7.5, 20°C
0.000764
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
pH 7.5, 20°C
0.084
(4R)-4-(ethylamino)-2-(3-methoxypropyl)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
-
pH 8.3, 20°C
0.0000063
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
pH 7.5, 20°C
0.0000929
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
pH 7.5, 20°C
0.00028
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
pH 7.5, 20°C
0.000806
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
pH 7.5, 20°C
0.079
(4S,6S)-4-(ethylamino)-6-methyl-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
-
pH 8.3, 20°C
0.000963
(4S,6S)-4-(ethylamino)-6-methyl-7,7-dioxo-4,5,6,7-tetrahydro-7lambda~6~-thieno[2,3-b]thiopyran-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA28
0.00794
(4S,6S)-4-(ethylamino)-6-methyl-7,7-dioxo-4,5,6,7-tetrahydro-7lambda~6~-thieno[2,3-b]thiopyran-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.000076
(5Z)-2-amino-5-(3,4-dihydroxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
-
isoform CA VB
0.000101
(5Z)-2-amino-5-(3,4-dihydroxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
-
isoform CA VA
0.0131
(5Z)-2-amino-5-(3,4-dihydroxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
-
isoform CA II
0.355
(5Z)-2-amino-5-(3,4-dihydroxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
-
isoform CA I
0.00007
(5Z)-2-amino-5-(4-hydroxy-3-methoxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
-
isoform CA VB
0.000099
(5Z)-2-amino-5-(4-hydroxy-3-methoxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
-
isoform CA VA
0.0096
(5Z)-2-amino-5-(4-hydroxy-3-methoxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
-
isoform CA II
0.0105
(5Z)-2-amino-5-(4-hydroxy-3-methoxybenzylidene)-3,5-dihydro-4H-imidazol-4-one
-
isoform CA I
0.0018
(heptadecafluorooctyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.007
(heptadecafluorooctyl)sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0000036
(R)- 4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000076
(R)- 4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.001207
(R)- 4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000334
(R)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0001334
(R)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.000205
(R)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000029
(R)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000218
(R)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
inhibition of isozyme, pH 9.0, 40°C
0.0000389
(R)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000198
(R)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000051
(R)-17(R)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000079
(R)-17(R)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000572
(R)-17(R)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.002626
(R)-17(R)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000669
(R)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.000176
(R)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0004557
(R)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.002639
(R)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000002
(R)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000075
(R)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000029
(R)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.000232
(R)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000023
(R)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000607
(R)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0003802
(R)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0004185
(R)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000019
(R)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000306
(R)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0000323
(R)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000181
(R)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000017
(R)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000039
(R)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0000054
(R)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.001811
(R)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000046
(R)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000154
(R)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000494
(R)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.001718
(R)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000033
(R)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.000032
(R)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000556
(R)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0002273
(R)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000004
(R)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000525
(R)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000539
(R)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.001659
(R)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000023
(R)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000029
(R)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.0000048
(R)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000166
(R)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000026
(R)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000066
(R)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.000007
(R)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.00152
(R)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000036
(R)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0000036
(R)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000076
(R)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.001207
(R)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000062
(R)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000087
(R)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000516
(R)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.00036
(R)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0003425
(S)- 4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0003586
(S)- 4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.001432
(S)- 4-(2-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000078
(S)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000613
(S)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000227
(S)- 4-(4-benzoyl-2-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000006
(S)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000077
(S)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000096
(S)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
inhibition of isozyme, pH 9.0, 40°C
0.00017
(S)-1-[4-(benzenesulfonyl)-2-benzylpiperazin-1-yl]ethan-1-one
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000279
(S)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000046
(S)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000793
(S)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000889
(S)-4-(2,4-dibenzylpiperazine-1-carbonyl)benzenesulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.0000316
(S)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000725
(S)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.000161
(S)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000186
(S)-4-(2-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.0000083
(S)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000221
(S)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0000733
(S)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.00025
(S)-4-(3,4-dibenzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000006
(S)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000079
(S)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0000744
(S)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000797
(S)-4-(3-benzyl-4-methanesulfonylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.000146
(S)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0003278
(S)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0005686
(S)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.001716
(S)-4-(3-benzyl-4-methylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000293
(S)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000607
(S)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0000834
(S)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000225
(S)-4-(3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000076
(S)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000088
(S)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0000668
(S)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000837
(S)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000015
(S)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000307
(S)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.000068
(S)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.000245
(S)-4-(4-benzoyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000054
(S)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000068
(S)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000295
(S)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.000191
(S)-4-[2-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000002
(S)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000061
(S)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.000104
(S)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000139
(S)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000927
(S)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000177
(S)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.000371
(S)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0005426
(S)-4-[3-benzyl-4-(2-phenylacetyl)piperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.0000078
(S)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000593
(S)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000083
(S)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0003303
(S)-4-[4-(benzenesulfonyl)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.0000622
(S)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000951
(S)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.000245
(S)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA I, pH 9.0, 40°C
0.001589
(S)-4-[4-(benzenesulfonyl)-3-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.005
(S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate
pH 7.5, 22°C
0.0711
(S)-benzyl (1-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-1-oxopropan-2-yl)carbamate
pH 7.5, 22°C
0.000029
1,2:3,4-di-O-isopropylidene-alpha-D-galactopyranose 6-sulfamate
-
pH 7.4, 25°C, hCA II
0.000032
1,2:3,4-di-O-isopropylidene-alpha-D-galactopyranose 6-sulfamate
-
pH 7.4, 25°C, hCA IX
0.000315
1,2:3,4-di-O-isopropylidene-alpha-D-galactopyranose 6-sulfamate
-
pH 7.4, 25°C, hCA I
0.000015
1,2:5,6-di-O-isopropylidene-alpha-D-glucofuranose 3-sulfamate
-
pH 7.4, 25°C, hCA II
0.000039
1,2:5,6-di-O-isopropylidene-alpha-D-glucofuranose 3-sulfamate
-
pH 7.4, 25°C, hCA IX
0.000278
1,2:5,6-di-O-isopropylidene-alpha-D-glucofuranose 3-sulfamate
-
pH 7.4, 25°C, hCA I
0.1664
1,3-dimethylpyrimidine-2,4(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.3162
1,3-dimethylpyrimidine-2,4(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.00015
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00019
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.105
1,5-bis[amino(dihydroxy)-lambda4-sulfanyl]-2,3-dichlorobenzene
-
20°C, pH not specified in the publication
0.000246
1-(1,2-benzoxazol-3-yl)methanesulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA32
0.000982
1-(1,2-benzoxazol-3-yl)methanesulfonamide
-
pH 7.5, 20°C
0.00789
1-(1,2-benzoxazol-3-yl)methanesulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0000055
1-cyclohexyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0001
1-cyclohexyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000178
1-cyclohexyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00065
1-cyclohexyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0004
1-cyclopentyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00165
1-cyclopentyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0041
1-cyclopentyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.35
1-cyclopentyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000047
1-cyclopropyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000061
1-cyclopropyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000105
1-cyclopropyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00378
1-cyclopropyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000064
1-n-butyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000085
1-n-butyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00082
1-n-butyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00395
1-n-butyl-6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000048
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0031
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0032
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0032
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0041
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0056
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0062
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0077
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0081
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0082
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0089
1-[(2-oxo-2H-chromen-6-yl)methyl]-3,5,7-triaza-1-azoniatricyclo[3.3.1.13,7]decane
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.00046
1-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-4-(4-sulfamoylphenyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0044
1-[2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl]-4-(4-sulfamoylphenyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00027
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.0013
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0257
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]ethanamine
-
20°C, pH not specified in the publication
0.00035
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.0085
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0285
1-[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]methanamine
-
20°C, pH not specified in the publication
0.0000065
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-galactopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000072
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-galactopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.000076
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-galactopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.008637
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-galactopyranosylamine
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.0000054
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-glucopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000077
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-glucopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.000081
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-glucopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.003714
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-glucopyranosylamine
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.000005
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-mannopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0000056
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-mannopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.000085
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-mannopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.009703
2,3,4,6-tetra-O-acetyl-N-sulfamoyl-beta-D-mannopyranosylamine
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.0000053
2,3,4-tri-O-acetyl-6-deoxy-N-sulfamoyl-alpha-L-glucopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0000058
2,3,4-tri-O-acetyl-6-deoxy-N-sulfamoyl-alpha-L-glucopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.000082
2,3,4-tri-O-acetyl-6-deoxy-N-sulfamoyl-alpha-L-glucopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.00953
2,3,4-tri-O-acetyl-6-deoxy-N-sulfamoyl-alpha-L-glucopyranosylamine
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.00083
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00095
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.05
2,4-bis[amino(dihydroxy)-lamba4-sulfanyl]-5-(trifluoromethyl)aniline
-
20°C, pH not specified in the publication
0.00012
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00061
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0621
2,4-bis[amino(dihydroxy)-lambda4-sulfanyl]-5-chloroaniline
-
20°C, pH not specified in the publication
0.000084
2-(3-chloro-4-hydroxyphenyl)-N-(2-methoxyethyl)acetamide
-
isoform CA VB
0.000102
2-(3-chloro-4-hydroxyphenyl)-N-(2-methoxyethyl)acetamide
-
isoform CA VA
0.000091
2-(3-chloro-4-hydroxyphenyl)-N-(2-phenylethyl)acetamide
-
isoform CA VB
0.000101
2-(3-chloro-4-hydroxyphenyl)-N-(2-phenylethyl)acetamide
-
isoform CA VA
0.000079
2-(3-chloro-4-hydroxyphenyl)-N-[2-(3,4-dimethoxyphenyl)ethyl]acetamide
-
isoform CA VB
0.000094
2-(3-chloro-4-hydroxyphenyl)-N-[2-(3,4-dimethoxyphenyl)ethyl]acetamide
-
isoform CA VA
0.0115
2-(3-chloro-4-hydroxyphenyl)-N-[2-(3,4-dimethoxyphenyl)ethyl]acetamide
-
isoform CA II
0.0119
2-(3-chloro-4-hydroxyphenyl)-N-[2-(3,4-dimethoxyphenyl)ethyl]acetamide
-
isoform CA I
0.000087
2-(3-chloro-4-hydroxyphenyl)-N-[2-(3-methoxyphenyl)ethyl]acetamide
-
isoform CA VB
0.000103
2-(3-chloro-4-hydroxyphenyl)-N-[2-(3-methoxyphenyl)ethyl]acetamide
-
isoform CA VA
0.0108
2-(3-chloro-4-hydroxyphenyl)-N-[2-(3-methoxyphenyl)ethyl]acetamide
-
isoform CA II
0.0112
2-(3-chloro-4-hydroxyphenyl)-N-[2-(3-methoxyphenyl)ethyl]acetamide
-
isoform CA I
0.000018
2-(3-chloro-4-hydroxyphenyl)-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
isoform CA II
0.000069
2-(3-chloro-4-hydroxyphenyl)-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
isoform CA VB
0.000093
2-(3-chloro-4-hydroxyphenyl)-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
isoform CA VA
0.0007
2-(3-chloro-4-hydroxyphenyl)-N-[2-(4-sulfamoylphenyl)ethyl]acetamide
-
isoform CA I
0.00232
2-(3-hydroxyphenyl)ethyl (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00469
2-(3-hydroxyphenyl)ethyl (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.0054
2-(3-hydroxyphenyl)ethyl (2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.0023
2-(3-hydroxyphenyl)ethyl (2E)-3-(4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00574
2-(3-hydroxyphenyl)ethyl (2E)-3-(4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00609
2-(3-hydroxyphenyl)ethyl (2E)-3-(4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.0000009
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA VI
0.0000028
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA VII
0.000003
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA II
0.000003
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA XII
0.000024
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA XIV
0.00003
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA VB
0.000037
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA IX
0.00005
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA VA
0.000128
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hpbetaCA
0.00021
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hpalphaCA
0.00046
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme gammaCA
45
2-(3-methoxypropyl)-4-(methylamino)-3,4-dihydro-2H-thieno[3,2-e][1,2]thiazine-6-sulfonamide 1,1-dioxide
isoenzyme hCA I
0.0032
2-(4-hydroxyphenyl)ethyl (2E)-3-(3-hydroperoxy-4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00567
2-(4-hydroxyphenyl)ethyl (2E)-3-(3-hydroperoxy-4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00726
2-(4-hydroxyphenyl)ethyl (2E)-3-(3-hydroperoxy-4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00187
2-(4-hydroxyphenyl)ethyl (2E)-3-(4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00467
2-(4-hydroxyphenyl)ethyl (2E)-3-(4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00513
2-(4-hydroxyphenyl)ethyl (2E)-3-(4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.0000072
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA II
0.0000072
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA II, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0000075
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA I
0.0000075
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA I, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000048
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA XIV catalytic domain
0.000048
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA XIV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000089
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA VII
0.000089
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA VII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000102
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA IX
0.000102
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA IX, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00011
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA XII
0.00011
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA XII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0011
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA VA
0.0011
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA VB
0.0011
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA VA, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0011
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA VB, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.002633
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme mCA XIII
0.00265
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA VI
0.00265
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA VI, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.009
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA IV
0.009
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA IV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
1.4
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isoenzyme hCA III
1.4
2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
isozyme CA III, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000893
2-(hydroxymethyl)-4-nitro-N-[2-(4-sulfamoylphenyl)ethyl]benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0128
2-(hydroxymethyl)-4-nitro-N-[2-(4-sulfamoylphenyl)ethyl]benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA21
0.0000502
2-(hydroxymethyl)-4-nitro-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
pH 7.5, 20°C
0.000134
2-(hydroxymethyl)-4-nitro-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
pH 7.5, 20°C
0.00001
2-(phenylethynyl)benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.00495
2-(phenylethynyl)benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.00637
2-(phenylethynyl)benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.806
2-(phenylethynyl)benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.0000315
2-adamantylethyl 7-methoxy-2-oxo-2H-chromene-8-carboxylate
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000639
2-adamantylethyl 7-methoxy-2-oxo-2H-chromene-8-carboxylate
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.000772
2-aminobenzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.005048
2-aminobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00587
2-aminobenzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00587
2-aminobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00624
2-aminobenzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00923
2-aminobenzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00923
2-aminobenzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00109
2-hydrazinobenzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.001035
2-hydrazinylbenzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.001035
2-hydrazinylbenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00251
2-hydrazinylbenzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.005639
2-hydrazinylbenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.0000879
2-methoxy-N-[(1-methylpyrrolidin-2-yl)methyl]-5-sulfamoylbenzamide
-
pH 7.5, 20°C
0.00032
2-methoxy-N-[(1-methylpyrrolidin-2-yl)methyl]-5-sulfamoylbenzamide
-
pH 8.3, 20°C
0.000378
2-methoxy-N-[(1-methylpyrrolidin-2-yl)methyl]-5-sulfamoylbenzamide
-
pH 7.5, 20°C
0.001
2-methoxy-N-[(1-methylpyrrolidin-2-yl)methyl]-5-sulfamoylbenzamide
-
pH 7.5, 20°C
0.00117
2-methoxy-N-[(1-methylpyrrolidin-2-yl)methyl]-5-sulfamoylbenzamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA33
0.00835
2-methoxy-N-[(1-methylpyrrolidin-2-yl)methyl]-5-sulfamoylbenzamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.1
2-methoxy-N-[(1-methylpyrrolidin-2-yl)methyl]-5-sulfamoylbenzamide
-
pH 7.5, 20°C
0.00000061
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA VII
0.0000077
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA XII
0.0000171
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA II
0.00002
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme mCA XIII
0.0000235
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA IV
0.000039
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA IX
0.000121
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA I
0.000438
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA VA
0.001422
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA VB
0.00215
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA VI
0.0029
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA XIV
0.36
2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide
isoenzyme hCA III
0.000012
2-N-(4-sulfamoylphenyl)-thioformyl-L-Ala
-
pH 7.5, carbonic anhydrase II
0.000006
2-N-(4-sulfamoylphenyl)-thioformyl-L-Asn
-
pH 7.5, carbonic anhydrase II
0.000027
2-N-(4-sulfamoylphenyl)-thioformyl-L-Asn
-
pH 7.5, carbonic anhydrase I
0.000009
2-N-(4-sulfamoylphenyl)-thioformyl-L-Gln
-
pH 7.5, carbonic anhydrase II
0.000004
2-N-(4-sulfamoylphenyl)-thioformyl-L-Ile
-
pH 7.5, carbonic anhydrase II
0.000022
2-N-(4-sulfamoylphenyl)-thioformyl-L-Ile
-
pH 7.5, carbonic anhydrase I
0.000005
2-N-(4-sulfamoylphenyl)-thioformyl-L-Leu
-
pH 7.5, carbonic anhydrase II
0.000021
2-N-(4-sulfamoylphenyl)-thioformyl-L-Leu
-
pH 7.5, carbonic anhydrase I
0.000004
2-N-(4-sulfamoylphenyl)-thioformyl-L-Met
-
pH 7.5, carbonic anhydrase II
0.000027
2-N-(4-sulfamoylphenyl)-thioformyl-L-Met
-
pH 7.5, carbonic anhydrase I
0.000006
2-N-(4-sulfamoylphenyl)-thioformyl-L-Phe
-
pH 7.5, carbonic anhydrase II
0.000025
2-N-(4-sulfamoylphenyl)-thioformyl-L-Pro
-
pH 7.5, carbonic anhydrase II
0.000011
2-N-(4-sulfamoylphenyl)-thioformyl-L-Trp
-
pH 7.5, carbonic anhydrase II
0.000047
2-N-(4-sulfamoylphenyl)-thioformyl-L-Trp
-
pH 7.5, carbonic anhydrase I
0.000005
2-N-(4-sulfamoylphenyl)-thioformyl-L-Val
-
pH 7.5, carbonic anhydrase II
0.000023
2-N-(4-sulfamoylphenyl)-thioformyl-L-Val
-
pH 7.5, carbonic anhydrase I
0.0038
2-oxo-2H-chromene-3-carboxylic acid
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0047
2-oxo-2H-chromene-3-carboxylic acid
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0051
2-oxo-2H-chromene-3-carboxylic acid
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0068
2-oxo-2H-chromene-3-carboxylic acid
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0074
2-oxo-2H-chromene-3-carboxylic acid
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.009
2-oxo-2H-chromene-3-carboxylic acid
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.009
2-oxo-2H-chromene-3-carboxylic acid
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0091
2-oxo-2H-chromene-3-carboxylic acid
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0093
2-oxo-2H-chromene-3-carboxylic acid
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0313
2-oxo-2H-chromene-3-carboxylic acid
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0447
2-oxo-2H-chromene-3-carboxylic acid
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000047
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0001
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0041
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0062
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0073
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0074
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0075
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0084
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0087
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0088
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.009
2-oxo-2H-thiochromene-3-carboxylic acid
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.00395
2-[3-[2-(3-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00683
2-[3-[2-(3-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00803
2-[3-[2-(3-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.0051
2-[4-[2-(4-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00532
2-[4-[2-(4-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00713
2-[4-[2-(4-hydroxyphenyl)ethoxy]phenyl]ethyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.0031
2H-chromen-2-one
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0092
2H-chromen-2-one
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0622
2H-chromen-2-one
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
2H-chromen-2-one
IC50 above 0.5 mM, isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
2H-chromen-2-one
IC50 above 0.5 mM, isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
2H-chromen-2-one
IC50 above 0.5 mM, isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
2H-chromen-2-one
IC50 above 0.5 mM, isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
2H-chromen-2-one
IC50 above 0.5 mM, isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
2H-chromen-2-one
IC50 above 0.5 mM, isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
2H-chromen-2-one
IC50 above 0.5 mM, isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
2H-chromen-2-one
IC50 above 0.5 mM, isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0000048
3,4,6-tri-O-acetyl-2-deoxy-N-sulfamoyl-beta-D-arabino-hexopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.000012
3,4,6-tri-O-acetyl-2-deoxy-N-sulfamoyl-beta-D-arabino-hexopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.000013
3,4,6-tri-O-acetyl-2-deoxy-N-sulfamoyl-beta-D-arabino-hexopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.00083
3,4,6-tri-O-acetyl-2-deoxy-N-sulfamoyl-beta-D-arabino-hexopyranosylamine
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.0000078
3,4,6-tri-O-acetyl-2-deoxy-N-sulfamoyl-beta-D-lyxo-hexopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.000011
3,4,6-tri-O-acetyl-2-deoxy-N-sulfamoyl-beta-D-lyxo-hexopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.000016
3,4,6-tri-O-acetyl-2-deoxy-N-sulfamoyl-beta-D-lyxo-hexopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.00083
3,4,6-tri-O-acetyl-2-deoxy-N-sulfamoyl-beta-D-lyxo-hexopyranosylamine
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.000006
3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000328
3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000037
3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00151
3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000957
3,5-dichloro-2-hydroxybenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00631
3,5-dichloro-2-hydroxybenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA10
0.000256
3-(4-sulfamoylphenyl)propanoic acid
-
in 10 mM HEPES (pH 7.4), at 25°C
0.00783
3-(4-sulfamoylphenyl)propanoic acid
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00793
3-(4-sulfamoylphenyl)propanoic acid
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00793
3-(4-sulfamoylphenyl)propanoic acid
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000057
3-(methylsulfanyl)-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.00015
3-(methylsulfanyl)-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.00051
3-(methylsulfanyl)-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.0000013
3-(phenylethynyl)benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.0000069
3-(phenylethynyl)benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.000059
3-(phenylethynyl)benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.000087
3-(phenylethynyl)benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.000581
3-aminobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA1
0.00063
3-aminobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.000033
3-chloro-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.00066
3-chloro-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.001
3-chloro-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.000009
3-morpholin-4-yl-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.00021
3-morpholin-4-yl-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.00021
3-morpholin-4-yl-4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.000012
3-phenylpropanenitrile
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.004125
3-phenylpropanenitrile
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.00845
3-phenylpropanenitrile
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.416
3-phenylpropanenitrile
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.000001
3-[(3-fluorophenyl)ethynyl]benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.000057
3-[(3-fluorophenyl)ethynyl]benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.000078
3-[(3-fluorophenyl)ethynyl]benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.00214
3-[(3-fluorophenyl)ethynyl]benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.0000017
3-[(3-methoxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.0000092
3-[(3-methoxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.000076
3-[(3-methoxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.006315
3-[(3-methoxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.0000011
3-[(4-methylphenyl)ethynyl]benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.000102
3-[(4-methylphenyl)ethynyl]benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.00041
3-[(4-methylphenyl)ethynyl]benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.00171
3-[(4-methylphenyl)ethynyl]benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.00001
3-[(anilinocarbonyl)amino]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000014
3-[(anilinocarbonyl)amino]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00145
3-[(anilinocarbonyl)amino]benzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.00017
3-[amino(dihydroxy)-lambda4-sulfanyl]aniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00124
3-[amino(dihydroxy)-lambda4-sulfanyl]aniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0143
3-[amino(dihydroxy)-lambda4-sulfanyl]aniline
-
20°C, pH not specified in the publication
0.00007
3-[[(aminosulfonyl)amino]sulfonyl]benzoic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0008
3-[[(aminosulfonyl)amino]sulfonyl]benzoic acid
-
pH 7.4, 25°C, isozyme hCA II
0.001
3-[[(aminosulfonyl)amino]sulfonyl]benzoic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0000047
4,4'-thiodipyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000473
4,4'-thiodipyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000065
4,4'-thiodipyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00016
4,4'-thiodipyridine-3-sulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.01117
4,4'-thiodipyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000069
4,4'-[(1R,2R,3S,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
-
isoform CA VB
0.000091
4,4'-[(1R,2R,3S,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
-
isoform CA VA
0.0117
4,4'-[(1R,2R,3S,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
-
isoform CA II
0.368
4,4'-[(1R,2R,3S,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
-
isoform CA I
0.000079
4,4'-[(1R,2S,3R,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
-
isoform CA VB
0.000098
4,4'-[(1R,2S,3R,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
-
isoform CA VA
0.0121
4,4'-[(1R,2S,3R,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
-
isoform CA II
0.354
4,4'-[(1R,2S,3R,4S)-3,4-dimethylcyclobutane-1,2-diyl]bis(2-methoxyphenol)
-
isoform CA I
0.000071
4,4'-[(2R,3R)-2,3-dimethylbutane-1,4-diyl]bis(2-methoxyphenol)
-
isoform CA VB
0.000085
4,4'-[(2R,3R)-2,3-dimethylbutane-1,4-diyl]bis(2-methoxyphenol)
-
isoform CA VA
0.23
4,4'-[(2R,3R)-2,3-dimethylbutane-1,4-diyl]bis(2-methoxyphenol)
-
isoform CA II
0.307
4,4'-[(2R,3R)-2,3-dimethylbutane-1,4-diyl]bis(2-methoxyphenol)
-
isoform CA I
0.000021
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA VB, i.e. daranide
0.000023
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme mCA XIII, i.e. daranide
0.000026
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA VII, i.e. daranide
0.000038
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA II, i.e. daranide
0.00005
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA IX, i.e. daranide
0.00005
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA XII, i.e. daranide
0.000079
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA VI, i.e. daranide
0.000105
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hpbetaCA, i.e. daranide
0.00019
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme gammaCA, i.e. daranide
0.000345
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA XIV, i.e. daranide
0.000378
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hpalphaCA, i.e. daranide
0.00063
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA VA, i.e. daranide
0.000872
4,5-dichloro-benzene-1,3-disulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0012
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA I, i.e. daranide
0.0063
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA III, i.e. daranide
0.015
4,5-dichloro-benzene-1,3-disulfonamide
isoenzyme hCA IV, i.e. daranide
0.000038
4,5-dichlorobenzene-1,3-disulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.00005
4,5-dichlorobenzene-1,3-disulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.00005
4,5-dichlorobenzene-1,3-disulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.000542
4,5-dichlorobenzene-1,3-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA27
0.00089
4,5-dichlorobenzene-1,3-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0000719
4-(1,1-dioxido-1,2-thiazinan-2-yl)benzenesulfonamide
-
pH 7.5, 20°C
0.0000884
4-(1,1-dioxido-1,2-thiazinan-2-yl)benzenesulfonamide
-
pH 7.5, 20°C
0.000276
4-(1,1-dioxido-1,2-thiazinan-2-yl)benzenesulfonamide
-
pH 7.5, 20°C
0.000834
4-(1,1-dioxido-1,2-thiazinan-2-yl)benzenesulfonamide
-
pH 7.5, 20°C
0.000132
4-(1,1-dioxo-1lambda6,2-thiazinan-2-yl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA37
0.0189
4-(1,1-dioxo-1lambda6,2-thiazinan-2-yl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0000051
4-(1,3,4-thiadiazol-2-ylthio)pyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000077
4-(1,3,4-thiadiazol-2-ylthio)pyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000569
4-(1,3,4-thiadiazol-2-ylthio)pyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00667
4-(1,3,4-thiadiazol-2-ylthio)pyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000042
4-(1-methyl-5-tetrazolylthio)pyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000046
4-(1-methyl-5-tetrazolylthio)pyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000458
4-(1-methyl-5-tetrazolylthio)pyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00653
4-(1-methyl-5-tetrazolylthio)pyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000151
4-(2-amino-pyrimidin-4-yl)-benzenesulfonamide
-
pH not specified in the publication, temperature not specified in the publication
0.003887
4-(2-amino-pyrimidin-4-yl)-benzenesulfonamide
-
at 20°C, pH 8.3
0.000758
4-(2-aminoethyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA6
0.0064
4-(2-aminoethyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0000943
4-(2-aminoethyl)benzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000577
4-(2-aminoethyl)benzenesulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000813
4-(2-aminoethyl)benzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.00088
4-(2-aminoethyl)benzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00088
4-(2-aminoethyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00342
4-(2-aminoethyl)benzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00856
4-(2-aminoethyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00956
4-(2-aminoethyl)benzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00956
4-(2-aminoethyl)benzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000726
4-(2-hydroxyethyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA17
0.000904
4-(2-hydroxyethyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00077
4-(2-hydroxyethyl)benzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000865
4-(2-hydroxyethyl)benzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000865
4-(2-hydroxyethyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00251
4-(2-hydroxyethyl)benzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00415
4-(2-hydroxyethyl)benzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.00513
4-(2-hydroxyethyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00551
4-(2-hydroxyethyl)benzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00551
4-(2-hydroxyethyl)benzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0000067
4-(2-methyl-8-quinolinoxy)-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00007
4-(2-methyl-8-quinolinoxy)-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000804
4-(2-methyl-8-quinolinoxy)-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000313
4-(2-methyl-8-quinolinoxy)-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.01032
4-(2-methyl-8-quinolinoxy)-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000012
4-(2-methylphenyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.00002
4-(2-methylphenyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.000047
4-(2-methylphenyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.0035
4-(2-methylphenyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.0000063
4-(2-propynylthio)pyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000156
4-(2-propynylthio)pyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000564
4-(2-propynylthio)pyridine-3-sulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000108
4-(2-propynylthio)pyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00832
4-(2-propynylthio)pyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000006
4-(3-formylphenyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.000002
4-(3-formylphenyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.000099
4-(3-formylphenyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.0012
4-(3-formylphenyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.0000002
4-(3-quinolinyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.0000025
4-(3-quinolinyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.000035
4-(3-quinolinyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.00076
4-(3-quinolinyl)benzene-1-sulfonamide
pH and temperature not specified in the publication
0.00003
4-(4'-dimethylaminophenyl)diazenylbenzenesulfonamide
-
isozyme CA VII, at 25°C, pH 7.4
0.000638
4-(4'-dimethylaminophenyl)diazenylbenzenesulfonamide
-
isozyme CA II, at 25°C, pH 7.4
0.000312
4-(4'-hydroxyphenyl)diazenylbenzene-N,N-dimethylsulfonamide
-
isozyme CA II, at 25°C, pH 7.4
0.000752
4-(4'-hydroxyphenyl)diazenylbenzene-N,N-dimethylsulfonamide
-
isozyme CA VII, at 25°C, pH 7.4
0.000277
4-(4'-hydroxyphenyl)diazenylbenzene-N-methylsulfonamide
-
isozyme CA II, at 25°C, pH 7.4
0.000706
4-(4'-hydroxyphenyl)diazenylbenzene-N-methylsulfonamide
-
isozyme CA VII, at 25°C, pH 7.4
0.000046
4-(4'-hydroxyphenyl)diazenylbenzenesulfonamide
-
isozyme CA VII, at 25°C, pH 7.4
0.000665
4-(4'-hydroxyphenyl)diazenylbenzenesulfonamide
-
isozyme CA II, at 25°C, pH 7.4
0.000863
4-(4'-methoxyphenyl)diazenylbenzene-N,N-dimethylsulfonamide
-
isozyme CA II, at 25°C, pH 7.4
0.0042
4-(4'-methoxyphenyl)diazenylbenzene-N,N-dimethylsulfonamide
-
isozyme CA VII, at 25°C, pH 7.4
0.0000063
4-(4-cyanophenoxy)-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000072
4-(4-cyanophenoxy)-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000945
4-(4-cyanophenoxy)-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00664
4-(4-cyanophenoxy)-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000069
4-(4-fluorophenoxy)-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000079
4-(4-fluorophenoxy)-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000944
4-(4-fluorophenoxy)-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00916
4-(4-fluorophenoxy)-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000078
4-(5-methyl-2-pyrazolino)-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000157
4-(5-methyl-2-pyrazolino)-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00014
4-(5-methyl-2-pyrazolino)-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000152
4-(5-methyl-2-pyrazolino)-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0103
4-(5-methyl-2-pyrazolino)-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000226
4-(5-methyl-3-phenyl-1,2-oxazol-4-yl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA35
0.0164
4-(5-methyl-3-phenyl-1,2-oxazol-4-yl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0000897
4-(5-methyl-3-phenyl-1,2-oxazol-4-yl)benzenesulfonamide
-
pH 7.5, 20°C
0.0000911
4-(5-methyl-3-phenyl-1,2-oxazol-4-yl)benzenesulfonamide
-
pH 7.5, 20°C
0.000517
4-(5-methyl-3-phenyl-1,2-oxazol-4-yl)benzenesulfonamide
-
pH 7.5, 20°C
0.000705
4-(5-methyl-3-phenyl-1,2-oxazol-4-yl)benzenesulfonamide
-
pH 7.5, 20°C
0.0315
4-(5-methyl-3-phenyl-1,2-oxazol-4-yl)benzenesulfonamide
-
pH 8.3, 20°C
0.00000216
4-(6-nitrobenzothiazol-2-ylthio)pyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000096
4-(6-nitrobenzothiazol-2-ylthio)pyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000948
4-(6-nitrobenzothiazol-2-ylthio)pyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00884
4-(6-nitrobenzothiazol-2-ylthio)pyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000012
4-(allylamino)-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000169
4-(allylamino)-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000133
4-(allylamino)-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000143
4-(allylamino)-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00886
4-(allylamino)-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000904
4-(aminomethyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00365
4-(aminomethyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA5
0.0000825
4-(aminomethyl)benzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000508
4-(aminomethyl)benzenesulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000768
4-(aminomethyl)benzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000768
4-(aminomethyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.0048
4-(aminomethyl)benzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.00591
4-(aminomethyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00733
4-(aminomethyl)benzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00869
4-(aminomethyl)benzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00869
4-(aminomethyl)benzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000012
4-(aminosulfonyl)-N-[2-[4-(aminosulfonyl)phenyl]ethyl]benzamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000013
4-(aminosulfonyl)-N-[2-[4-(aminosulfonyl)phenyl]ethyl]benzamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000025
4-(aminosulfonyl)-N-[2-[4-(aminosulfonyl)phenyl]ethyl]benzamide
-
pH 7.5, 20°C
0.000079
4-(aminosulfonyl)-N-[2-[4-(aminosulfonyl)phenyl]ethyl]benzamide
pH 7.5, full-length recombinant enzyme
1.06
4-(aminosulfonyl)-N-[2-[4-(aminosulfonyl)phenyl]ethyl]benzamide
20°C, pH 7.5
0.000887
4-(aminosulfonyl)benzoic acid
20°C, pH 7.5, full-length recombinant hCA VI
0.0000118
4-(carbamoylmethylthio)pyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000159
4-(carbamoylmethylthio)pyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000131
4-(carbamoylmethylthio)pyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000142
4-(carbamoylmethylthio)pyridine-3-sulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00951
4-(carbamoylmethylthio)pyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000117
4-(cyanomethylthio)pyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000155
4-(cyanomethylthio)pyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000911
4-(cyanomethylthio)pyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00014
4-(cyanomethylthio)pyridine-3-sulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.01171
4-(cyanomethylthio)pyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000704
4-(hydroxymethyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA16
0.0063
4-(hydroxymethyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.000754
4-(hydroxymethyl)benzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000754
4-(hydroxymethyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000758
4-(hydroxymethyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.000768
4-(hydroxymethyl)benzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.00668
4-(hydroxymethyl)benzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.00782
4-(hydroxymethyl)benzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00956
4-(hydroxymethyl)benzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00956
4-(hydroxymethyl)benzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0000089
4-(methylhydrazino)-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000158
4-(methylhydrazino)-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000872
4-(methylhydrazino)-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000957
4-(methylhydrazino)-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000562
4-(methylhydrazino)-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000075
4-(N-oxide-2-pyridylthio)pyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000138
4-(N-oxide-2-pyridylthio)pyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000845
4-(N-oxide-2-pyridylthio)pyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00762
4-(N-oxide-2-pyridylthio)pyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000094
4-(phenylethynyl)benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.000069
4-(phenylethynyl)benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.0052
4-(phenylethynyl)benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.00565
4-(phenylethynyl)benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.0000068
4-(quinolinoxy)-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000091
4-(quinolinoxy)-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000597
4-(quinolinoxy)-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000105
4-(quinolinoxy)-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.01032
4-(quinolinoxy)-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0025
4-acetyl-N-(aminosulfonyl)benzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.0036
4-acetyl-N-(aminosulfonyl)benzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.00006
4-amino-3,5-dibromobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.000243
4-amino-3,5-dibromobenzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000243
4-amino-3,5-dibromobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00054
4-amino-3,5-dibromobenzenesulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000084
4-amino-3,5-diiodobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.000345
4-amino-3,5-diiodobenzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000345
4-amino-3,5-diiodobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000695
4-amino-3,5-diiodobenzenesulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.00502
4-amino-3-bromobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00544
4-amino-3-bromobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA9
0.000104
4-amino-3-bromobenzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000186
4-amino-3-bromobenzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000186
4-amino-3-bromobenzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00468
4-amino-3-bromobenzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.00732
4-amino-3-bromobenzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.006175
4-amino-3-chlorobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA8
0.0113
4-amino-3-chlorobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.000079
4-amino-3-chlorobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.0000875
4-amino-3-chlorobenzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000551
4-amino-3-chlorobenzenesulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.0008
4-amino-3-chlorobenzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.0008
4-amino-3-chlorobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.001097
4-amino-3-chlorobenzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.00151
4-amino-3-chlorobenzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00752
4-amino-3-chlorobenzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00752
4-amino-3-chlorobenzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.005545
4-amino-3-fluorobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA7
0.0102
4-amino-3-fluorobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0000751
4-amino-3-fluorobenzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000083
4-amino-3-fluorobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.000096
4-amino-3-fluorobenzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.000493
4-amino-3-fluorobenzenesulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.00107
4-amino-3-fluorobenzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00107
4-amino-3-fluorobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.0079
4-amino-3-fluorobenzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00874
4-amino-3-fluorobenzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00874
4-amino-3-fluorobenzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0000883
4-amino-3-iodobenzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.001024
4-amino-3-iodobenzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.00581
4-amino-3-iodobenzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00771
4-amino-3-iodobenzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00771
4-amino-3-iodobenzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0000629
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
pH 7.5, 20°C
0.000087
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00009
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
pH 8.3, 20°C
0.000367
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000481
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000552
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
pH 7.5, 20°C
0.000842
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
pH 7.5, 20°C
0.000926
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
at 20°C and pH 7.5
0.000955
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.00235
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0025
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00483
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00483
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.0081
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0081
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.009083
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
-
pH 7.5, 20°C
0.01245
4-amino-6-(trifluoromethyl)benzene-1,3-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA11
0.0000453
4-amino-6-chlorobenzene-1,3-disulfonamide
-
pH 7.5, 20°C
0.000295
4-amino-6-chlorobenzene-1,3-disulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000608
4-amino-6-chlorobenzene-1,3-disulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.000691
4-amino-6-chlorobenzene-1,3-disulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00084
4-amino-6-chlorobenzene-1,3-disulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.00094
4-amino-6-chlorobenzene-1,3-disulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00094
4-amino-6-chlorobenzene-1,3-disulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00172
4-amino-6-chlorobenzene-1,3-disulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00172
4-amino-6-chlorobenzene-1,3-disulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00414
4-amino-6-chlorobenzene-1,3-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA12
0.0054
4-amino-6-chlorobenzene-1,3-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0217
4-amino-6-chlorobenzene-1,3-disulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0736
4-amino-6-chlorobenzene-1,3-disulfonamide
-
pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity
0.0000298
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.0000427
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
pH 7.5, 20°C
0.000048
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
pH 7.5, 20°C
0.000049
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
at 20°C and pH 7.5
0.000094
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00018
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.000612
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000612
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000868
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.00105
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00105
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00221
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00636
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0524
4-amino-N-(4-sulfamoylbenzyl)benzenesulfonamide
-
20°C, pH not specified in the publication
0.006705
4-amino-N-(4-sulfamoylcyclopenta-1,3-dien-1-yl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA20
0.0124
4-amino-N-(4-sulfamoylcyclopenta-1,3-dien-1-yl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00814
4-amino-N-(4-sulfamoylphenyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.015
4-amino-N-(4-sulfamoylphenyl)benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA22
0.0000042
4-amino-N-(4-sulfamoylphenyl)benzenesulfonamide
-
pH 7.5, 20°C
0.0146
4-amino-N-[(4-sulfamoylphenyl)methyl]benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA23
-
0.0187
4-amino-N-[(4-sulfamoylphenyl)methyl]benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
-
0.0084
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA24
0.0212
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.000016
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
pH 7.5, 20°C
0.0000197
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.0000303
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
pH 7.5, 20°C
0.000063
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
at 20°C and pH 7.5
0.000063
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
pH 8.3, 20°C
0.000068
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.0000734
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
pH 7.5, 20°C
0.00017
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000192
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
pH 7.5, 20°C
0.00065
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000745
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000745
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000853
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000853
4-amino-N-[2-(4-sulfamoylphenyl)ethyl]benzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000024
4-amino-N-[2-[4-(aminosulfonyl)phenyl]ethyl]benzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.14
4-amino-N-[2-[4-(aminosulfonyl)phenyl]ethyl]benzenesulfonamide
20°C, pH 7.5
0.000055
4-amino-N-[4-(aminosulfonyl)benzyl]benzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.000808
4-aminobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0058
4-aminobenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA2
0.000037
4-Aminobenzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.00024
4-Aminobenzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.000294
4-Aminobenzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.000941
4-Aminobenzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.0025
4-Aminobenzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.0025
4-Aminobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00508
4-Aminobenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00711
4-Aminobenzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00984
4-Aminobenzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00984
4-Aminobenzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0000032
4-aminoethylbenzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000033
4-aminoethylbenzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.0029
4-aminoethylbenzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.0000065
4-benzythiopyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000099
4-benzythiopyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000304
4-benzythiopyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000682
4-benzythiopyridine-3-sulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00909
4-benzythiopyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000079
4-chlorophenyl sulfamate
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000215
4-chlorophenyl sulfamate
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.0000059
4-ethoxy-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000522
4-ethoxy-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000767
4-ethoxy-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0003
4-ethoxy-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0061
4-ethoxy-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000049
4-hydrazino-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000101
4-hydrazino-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000856
4-hydrazino-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000934
4-hydrazino-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00791
4-hydrazino-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.001275
4-hydrazinobenzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.0024
4-hydrazinylbenzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.0024
4-hydrazinylbenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.004763
4-hydrazinylbenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00289
4-hydroxybenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00449
4-hydroxybenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA15
0.0000057
4-methoxy-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000058
4-methoxy-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00009384
4-methoxy-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00734
4-methoxy-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00312
4-methylbenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00558
4-methylbenzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA4
0.0075
4-methylbenzene-1-sulfonamide
-
pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity
0.00158
4-methylbenzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00158
4-methylbenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.001582
4-methylbenzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.00492
4-methylbenzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00492
4-methylbenzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00556
4-methylbenzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00702
4-methylbenzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0000067
4-methylthiopyridine-3-sulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000401
4-methylthiopyridine-3-sulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000047
4-methylthiopyridine-3-sulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00903
4-methylthiopyridine-3-sulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00983
4-methylthiopyridine-3-sulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000002
4-phenylbenzene-1-sulfonamide
pH and temperature not specified in the publication
0.0000008
4-phenylbenzene-1-sulfonamide
pH and temperature not specified in the publication
0.000042
4-phenylbenzene-1-sulfonamide
pH and temperature not specified in the publication
0.000093
4-phenylbenzene-1-sulfonamide
pH and temperature not specified in the publication
0.000027
4-sulfamoyl-N-[2-(4-sulfamoylphenyl)ethyl]benzamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000027
4-sulfamoyl-N-[2-(4-sulfamoylphenyl)ethyl]benzamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000034
4-sulfamoyl-N-[2-(4-sulfamoylphenyl)ethyl]benzamide
-
pH 7.5, 20°C
0.00009
4-sulfamoyl-N-[2-(4-sulfamoylphenyl)ethyl]benzamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.000902
4-sulfamoyl-N-[2-(4-sulfamoylphenyl)ethyl]benzamide
-
isozyme STPCA, pH 7.5, 20°C
0.00034
4-sulfamoylbenzoic acid
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00034
4-sulfamoylbenzoic acid
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000697
4-sulfamoylbenzoic acid
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00678
4-sulfamoylbenzoic acid
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA18
0.0074
4-sulfamoylbenzoic acid
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0077
4-sulfamoylbenzoic acid
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00821
4-sulfamoylbenzoic acid
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00821
4-sulfamoylbenzoic acid
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00525
4-[(2-aminopyrimidin-4-yl)amino]benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA19
0.006225
4-[(2-aminopyrimidin-4-yl)amino]benzene-1-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.000021
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000021
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.0000254
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000054
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
-
pH 7.5, 20°C
0.0000598
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
-
pH 7.5, 20°C
0.000067
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
at 20°C and pH 7.5
0.000068
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
-
pH 8.3, 20°C
0.000086
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.000091
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000642
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.00075
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00075
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000769
4-[(2-aminopyrimidin-4-yl)amino]benzenesulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.0000056
4-[(2R)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.0000081
4-[(2R)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0000087
4-[(2R)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.001442
4-[(2R)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0000754
4-[(2S)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IV, pH 9.0, 40°C
0.000093
4-[(2S)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA IX, pH 9.0, 40°C
0.0002645
4-[(2S)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme hCA II, pH 9.0, 40°C
0.0004219
4-[(2S)-2-benzylpiperazine-1-carbonyl]benzene-1-sulfonamide
inhibition of isozyme, pH 9.0, 40°C
0.0000058
4-[(3-fluorophenyl)ethynyl]benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.000057
4-[(3-fluorophenyl)ethynyl]benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.000062
4-[(3-fluorophenyl)ethynyl]benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.000076
4-[(3-fluorophenyl)ethynyl]benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.0000016
4-[(3-hydroxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.000059
4-[(3-hydroxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.000087
4-[(3-hydroxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.00529
4-[(3-hydroxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.0000012
4-[(3-methoxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.0000065
4-[(3-methoxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.000078
4-[(3-methoxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.00489
4-[(3-methoxyphenyl)ethynyl]benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.000068
4-[(4-methylphenyl)ethynyl]benzenesulfonamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.000104
4-[(4-methylphenyl)ethynyl]benzenesulfonamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.00522
4-[(4-methylphenyl)ethynyl]benzenesulfonamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.00559
4-[(4-methylphenyl)ethynyl]benzenesulfonamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.000037
4-[(acetyloxy)amino]-N-[4-(aminosulfonyl)phenyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000076
4-[(acetyloxy)amino]-N-[4-(aminosulfonyl)phenyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00088
4-[(acetyloxy)amino]-N-[4-(aminosulfonyl)phenyl]benzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.0026
4-[(acetyloxy)amino]-N-[4-(aminosulfonyl)phenyl]benzenesulfonamide
-
pH 7.5, 20°C
0.000069
4-[(anilinocarbonyl)amino]-6-chlorobenzene-1,3-disulfonamide
-
pH 7.5, 20°C
0.000146
4-[(anilinocarbonyl)amino]-6-chlorobenzene-1,3-disulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000348
4-[(anilinocarbonyl)amino]-6-chlorobenzene-1,3-disulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00043
4-[(anilinocarbonyl)amino]-6-chlorobenzene-1,3-disulfonamide
pH 7.5, full-length recombinant enzyme
0.000033
4-[(methylsulfonyl)amino]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000113
4-[(methylsulfonyl)amino]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00125
4-[(methylsulfonyl)amino]benzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.000052
4-[(phenylsulfonyl)amino]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000068
4-[(phenylsulfonyl)amino]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000935
4-[(phenylsulfonyl)amino]benzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.0000075
4-[2-(4-sulfamoylphenyl)ethylamino]-3-pyridinosulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000151
4-[2-(4-sulfamoylphenyl)ethylamino]-3-pyridinosulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000052
4-[2-(4-sulfamoylphenyl)ethylamino]-3-pyridinosulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000149
4-[2-(4-sulfamoylphenyl)ethylamino]-3-pyridinosulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00152
4-[2-(4-sulfamoylphenyl)ethylamino]-3-pyridinosulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000021
4-[2-[(anilinocarbonothioyl)amino]ethyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000024
4-[2-[(anilinocarbonothioyl)amino]ethyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000203
4-[2-[(anilinocarbonothioyl)amino]ethyl]benzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.00298
4-[2-[(anilinocarbonothioyl)amino]ethyl]benzenesulfonamide
-
pH 7.5, 20°C
0.000013
4-[2-[(anilinocarbonyl)amino]ethyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000018
4-[2-[(anilinocarbonyl)amino]ethyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000039
4-[2-[(anilinocarbonyl)amino]ethyl]benzenesulfonamide
-
pH 7.5, 20°C
0.00026
4-[2-[(anilinocarbonyl)amino]ethyl]benzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.000003
4-[2-[([[4-(aminosulfonyl)phenyl]amino]carbonothioyl)amino]ethyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000079
4-[2-[([[4-(aminosulfonyl)phenyl]amino]carbonothioyl)amino]ethyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000085
4-[2-[([[4-(aminosulfonyl)phenyl]amino]carbonothioyl)amino]ethyl]benzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.00303
4-[2-[([[4-(aminosulfonyl)phenyl]amino]carbonothioyl)amino]ethyl]benzenesulfonamide
-
pH 7.5, 20°C
0.0000016
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-alpha-D-mannopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000021
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-alpha-D-mannopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000005
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-alpha-D-mannopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000087
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00011
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0043
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-galactopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000091
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00012
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0044
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4',6'-tetra-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000082
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-alpha-D-arabinopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000105
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-alpha-D-arabinopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000134
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-alpha-D-arabinopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000099
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000048
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00013
4-[4-(aminosulfonyl)phenyl]-1-(2',3',4'-tri-O-acetyl-beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0001
4-[4-(aminosulfonyl)phenyl]-1-(2',3',5'-tri-O-benzoyl-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000427
4-[4-(aminosulfonyl)phenyl]-1-(2',3',5'-tri-O-benzoyl-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0053
4-[4-(aminosulfonyl)phenyl]-1-(2',3',5'-tri-O-benzoyl-beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000101
4-[4-(aminosulfonyl)phenyl]-1-(2'-acetamido-2'-deoxy'-3',4',6'-tri-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00044
4-[4-(aminosulfonyl)phenyl]-1-(2'-acetamido-2'-deoxy'-3',4',6'-tri-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.005
4-[4-(aminosulfonyl)phenyl]-1-(2'-acetamido-2'-deoxy'-3',4',6'-tri-O-acetyl-beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000023
4-[4-(aminosulfonyl)phenyl]-1-(alpha-D-arabinopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000025
4-[4-(aminosulfonyl)phenyl]-1-(alpha-D-arabinopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000028
4-[4-(aminosulfonyl)phenyl]-1-(alpha-D-arabinopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000028
4-[4-(aminosulfonyl)phenyl]-1-(alpha-D-mannopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000054
4-[4-(aminosulfonyl)phenyl]-1-(alpha-D-mannopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000076
4-[4-(aminosulfonyl)phenyl]-1-(alpha-D-mannopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000093
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-galactopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000088
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-galactopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00012
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-galactopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000089
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000094
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00038
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-glucopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000084
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000013
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00056
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-glucuronic acid methyl ester)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00013
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-maltopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000432
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-maltopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.005
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-maltopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000075
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000121
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0043
4-[4-(aminosulfonyl)phenyl]-1-(beta-D-ribofuranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00012
4-[4-(aminosulfonyl)phenyl]-1-(hepta-O-acetyl-beta-D-maltopyranosyl)-1H-1,2,3-triazole
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000235
4-[4-(aminosulfonyl)phenyl]-1-(hepta-O-acetyl-beta-D-maltopyranosyl)-1H-1,2,3-triazole
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0025
4-[4-(aminosulfonyl)phenyl]-1-(hepta-O-acetyl-beta-D-maltopyranosyl)-1H-1,2,3-triazole
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000021
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
wild-type, pH 7.5, 20°C
0.0000827
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
pH 7.5, 20°C
0.000338
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
pH 7.5, 20°C
0.000732
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
pH 7.5, 20°C
0.001
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
pH 7.5, 20°C
0.0348
4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide
-
pH 8.3, 20°C
0.00028
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00172
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.077
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-bromoaniline
-
20°C, pH not specified in the publication
0.00014
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00074
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.111
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-chloroaniline
-
20°C, pH not specified in the publication
0.00097
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.0042
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0534
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-fluoroaniline
-
20°C, pH not specified in the publication
0.00028
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00066
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
20°C, pH not specified in the publication, Co2+-containing enzyme
0.098
4-[amino(dihydroxy)-lambda4-sulfanyl]-2-iodoaniline
-
20°C, pH not specified in the publication
0.0000046
4-[N'-(1,1-dioxopyrido[4,3-e]-1,4,2-dithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000161
4-[N'-(1,1-dioxopyrido[4,3-e]-1,4,2-dithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000837
4-[N'-(1,1-dioxopyrido[4,3-e]-1,4,2-dithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000117
4-[N'-(1,1-dioxopyrido[4,3-e]-1,4,2-dithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0089
4-[N'-(1,1-dioxopyrido[4,3-e]-1,4,2-dithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000034
4-[N'-(6-chloro-7-cyano-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000072
4-[N'-(6-chloro-7-cyano-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000078
4-[N'-(6-chloro-7-cyano-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000883
4-[N'-(6-chloro-7-cyano-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000923
4-[N'-(6-chloro-7-cyano-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazino]-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000058
4-[N'-(6-chloro-7-methyl-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazyno]-3-pyridinesulfonamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000461
4-[N'-(6-chloro-7-methyl-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazyno]-3-pyridinesulfonamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000509
4-[N'-(6-chloro-7-methyl-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazyno]-3-pyridinesulfonamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000101
4-[N'-(6-chloro-7-methyl-1,1-dioxo-1,4,2-benzodithiazin-3-yl)hydrazyno]-3-pyridinesulfonamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00006
4-[[(aminosulfonyl)amino]sulfonyl]benzoic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0007
4-[[(aminosulfonyl)amino]sulfonyl]benzoic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0009
4-[[(aminosulfonyl)amino]sulfonyl]benzoic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.000018
4-[[(anilinocarbonothioyl)amino]methyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000026
4-[[(anilinocarbonothioyl)amino]methyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000237
4-[[(anilinocarbonothioyl)amino]methyl]benzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.00297
4-[[(anilinocarbonothioyl)amino]methyl]benzenesulfonamide
-
pH 7.5, 20°C
0.00004
4-[[(phenylsulfonyl)amino]methyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000083
4-[[(phenylsulfonyl)amino]methyl]benzenesulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000465
4-[[(phenylsulfonyl)amino]methyl]benzenesulfonamide
pH 7.5, full-length recombinant enzyme
0.00046
4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.00072
4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.0021
4H-[1,2,3]thiadiazolo[3,4-a]benzimidazole-7-sulfonamide
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4
0.0001035
5,6-diamino-1,3-dimethyluracil
pH 7.4, temperature not specified in the publication
0.000236
5,6-diamino-1,3-dimethyluracil
pH 7.4, temperature not specified in the publication
0.000033
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000033
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00006
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
at 20°C and pH 7.5
0.000114
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.000166
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.000607
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000792
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.00748
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00748
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0076
5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00000059
5-(3-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.0000885
5-([(4-aminophenyl)sulfonyl]amino)-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.0000951
5-([(4-aminophenyl)sulfonyl]amino)-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.04188
5-([(4-aminophenyl)sulfonyl]amino)-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.025
5-acetamido-1,3,4-thiadiazole-2-sulfonamide
-
Escherichia coli recombinant enzyme
0.000105
5-amino-1,3,4-thiadiazole-2-sulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000361
5-amino-1,3,4-thiadiazole-2-sulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000618
5-amino-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA13
0.000675
5-amino-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.000798
5-amino-1,3,4-thiadiazole-2-sulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.000847
5-amino-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00121
5-amino-1,3,4-thiadiazole-2-sulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00121
5-amino-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00763
5-amino-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.01154
5-amino-1,3,4-thiadiazole-2-sulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.01154
5-amino-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.01083
5-bromo-1-(4-methylbenzene-1-sulfonyl)pyrimidine-2,4(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.02888
5-bromo-1-(4-methylbenzene-1-sulfonyl)pyrimidine-2,4(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.428
5-bromo-1-(methanesulfonyl)pyrimidine-2,4(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.645
5-bromo-1-(methanesulfonyl)pyrimidine-2,4(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.0000112
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.0000121
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.000049
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
at 20°C and pH 7.5
0.0000919
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000357
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000393
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.000433
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.000652
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.00074
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.000744
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA14
0.000912
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00143
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00143
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00792
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.01265
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.01265
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.085
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
pH 8.3, 20°C
0.198
5-imino-4-methyl-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
20°C, pH 7.5
0.00133
5-[(benzenesulfonyl)amino]-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA30
0.0112
5-[(benzenesulfonyl)amino]-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0000042
5-[(phenylsulfonyl)amino]-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.000032
5-[(phenylsulfonyl)amino]-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.0000936
5-[(phenylsulfonyl)amino]-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.000236
5-[(phenylsulfonyl)amino]-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.000482
5-[(phenylsulfonyl)amino]-1,3,4-thiadiazole-2-sulfonamide
-
pH 8.3, 20°C
0.000186
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.0805
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
20°C, pH 7.5
0.000186
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000661
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000663
5-[[(4-amino-3-chloro-5-fluorophenyl)sulfonyl]amino]-4,5-dihydro-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.0000276
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
in 10 mM HEPES (pH 7.4), at 25°C
0.000048
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
at 20°C and pH 7.5
0.00007
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.00007
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000073
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.000108
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.000333
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.000905
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000905
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA 1, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0031
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0181
5-[[(4-aminophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
20°C, pH 7.5
0.0000033
5-[[(4-bromophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000013
5-[[(4-bromophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, full-length recombinant enzyme
0.000021
5-[[(4-bromophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000062
5-[[(4-bromophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.0000019
5-[[(4-nitrophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00001
5-[[(4-nitrophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, full-length recombinant enzyme
0.000016
5-[[(4-nitrophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000072
5-[[(4-nitrophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
-
pH 7.5, 20°C
0.0000094
6,7-dimethoxy-1-ethyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000096
6,7-dimethoxy-1-ethyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000873
6,7-dimethoxy-1-ethyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0028
6,7-dimethoxy-1-ethyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000302
6,7-dimethoxy-1-isopropyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00033
6,7-dimethoxy-1-isopropyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00315
6,7-dimethoxy-1-isopropyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.235
6,7-dimethoxy-1-isopropyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000095
6,7-dimethoxy-1-methyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000098
6,7-dimethoxy-1-methyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000945
6,7-dimethoxy-1-methyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00641
6,7-dimethoxy-1-methyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00386
6,7-dimethoxy-1-phenyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00844
6,7-dimethoxy-1-phenyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00898
6,7-dimethoxy-1-phenyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0157
6,7-dimethoxy-1-phenyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000763
6,7-dimethoxy-1-propyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00182
6,7-dimethoxy-1-propyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.001975
6,7-dimethoxy-1-propyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.002754
6,7-dimethoxy-1-propyl-3,4-dihydroisoquinoline-2(1H)-sulfonamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000059
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA II, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000078
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA I, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0038
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA IV, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0078
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA XIV, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0177
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA VB, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0279
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA VII, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0357
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA VI, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0486
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA XII, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0545
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA IX, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.096
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
isoform CA VA, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
6-((1S)-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
Ki above 0.5 mM, isoform CA III, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0000486
6-(1-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000545
6-(1-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.000059
6-(1-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
-
inhibition of isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.000078
6-(1-hydroxy-3-methylbutyl)-7-methoxy-2H-chromen-2-one
-
inhibition of isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.0037
6-(aminomethyl)-2H-chromen-2-one
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0054
6-(aminomethyl)-2H-chromen-2-one
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0062
6-(aminomethyl)-2H-chromen-2-one
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0067
6-(aminomethyl)-2H-chromen-2-one
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0071
6-(aminomethyl)-2H-chromen-2-one
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0081
6-(aminomethyl)-2H-chromen-2-one
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0086
6-(aminomethyl)-2H-chromen-2-one
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0088
6-(aminomethyl)-2H-chromen-2-one
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0092
6-(aminomethyl)-2H-chromen-2-one
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0096
6-(aminomethyl)-2H-chromen-2-one
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0097
6-(aminomethyl)-2H-chromen-2-one
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0043
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0056
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0062
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0066
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0084
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0086
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0089
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0093
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0097
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0156
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0445
6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylic acid
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000093
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0051
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0068
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0069
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0078
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0082
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0089
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0095
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0098
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0099
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0324
6-(hydroxymethyl)-2H-chromen-2-one
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.00654
6-acetyl-7-methoxy-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0078
6-acetyl-7-methoxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.000085
6-amino-1,3-dimethyluracil
pH 7.4, temperature not specified in the publication
0.0001715
6-amino-1,3-dimethyluracil
pH 7.4, temperature not specified in the publication
0.0196
6-chloro-1,1-dioxo-1,2,3,4-tetrahydro-1lambda6,2,4-benzothiadiazine-7-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0683
6-chloro-1,1-dioxo-1,2,3,4-tetrahydro-1lambda6,2,4-benzothiadiazine-7-sulfonamide
-
pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity
0.0000502
6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide
-
pH 7.5, 20°C
0.0000795
6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide
-
pH 7.5, 20°C
0.000134
6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide
-
pH 7.5, 20°C
0.000394
6-chloro-3,4-dihydro-2H-1,2,4-benzothiadiazine-7-sulfonamide 1,1-dioxide
-
pH 7.5, 20°C
0.000039
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA IX
0.000044
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA XII
0.000049
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hpalphaCA
0.000075
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA II
0.00012
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme gammaCA
0.00021
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA VII
0.00038
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA IV
0.00057
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA XIV
0.000608
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA VI
0.00064
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hpbetaCA
0.00415
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA VA
0.0062
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA VB
0.0068
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA III
0.0084
6-chloro-4-amino-benzene-1,3-disulfonamide
isoenzyme hCA I
0.0000073
6-deoxy-N-(4-sulfamoylphenyl)-alpha-L-mannopyranosylamine
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.000019
6-deoxy-N-(4-sulfamoylphenyl)-alpha-L-mannopyranosylamine
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.00314
6-deoxy-N-sulfamoyl-alpha-L-glucopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0099
6-deoxy-N-sulfamoyl-alpha-L-glucopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0223
6-deoxy-N-sulfamoyl-alpha-L-glucopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.5
6-deoxy-N-sulfamoyl-alpha-L-glucopyranosylamine
-
above, isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.00000069
6-ethoxy-1,3-benzothiazole-2-sulfonamide
-
pH 7.5, 20°C
0.000131
6-ethoxy-1,3-benzothiazole-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA26
0.00075
6-ethoxy-1,3-benzothiazole-2-sulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.000025
6-ethoxy-2-benzo-thiazolesulfonamide
-
pH 7.0, 10°C, mutant H66A
0.000084
6-ethoxy-2-benzo-thiazolesulfonamide
-
pH 7.0, 10°C, wild-type enzyme
0.0000047
6-hydroxy-1,3-benzothiazole-2-sulfonamide
-
pH 7.5, 20°C
0.000048
6-hydroxy-1,3-benzothiazole-2-sulfonamide
isoform CA I, in 10-20 mM Tris, pH 8.3, 10-20 mM NaCl
0.000048
6-hydroxy-1,3-benzothiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000083
6-hydroxy-1,3-benzothiazole-2-sulfonamide
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.000103
6-hydroxy-1,3-benzothiazole-2-sulfonamide
20°C, pH 7.5, full-length recombinant hCA VI
0.000701
6-hydroxy-1,3-benzothiazole-2-sulfonamide
-
isozyme STPCA, pH 7.5, 20°C
0.0049
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0049
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0066
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0066
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0076
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0087
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.009
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0105
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0145
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0153
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0396
6-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0056
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0068
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0077
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0083
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
IC50 above 0.5 mM, isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0086
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0086
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.013
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0134
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0296
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0317
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0425
6-methyl-2-oxo-2H-chromene-3-carboxylic acid
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0000035
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA VII
0.0000035
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA XII
0.000009
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA II
0.00001
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA VI
0.000018
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme mCA XIII
0.000027
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA XIV
0.000033
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA VB
0.000042
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA VA
0.000052
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA IX
0.000073
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hpbetaCA
0.00041
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme gammaCA
0.00436
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hpalphaCA
0.0085
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA IV
0.05
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA I
8
6-methyl-4-(methylamino)-5,6-dihydro-4H-thieno[2,3-b]thiopyran-2-sulfonamide 7,7-dioxide
isoenzyme hCA III
0.00002
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme mCA XIII
0.000024
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA IX
0.000045
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA XII
0.000063
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA II
0.0001
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA VII
0.000412
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hpalphaCA
0.00068
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA XIV
0.00083
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme gammaCA
0.000955
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA VI
0.000973
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hpbetaCA
0.0048
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA IV
0.0058
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA I
0.0065
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA VB
0.0072
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA III
0.0094
6-trifluoromethyl-4-aminobenzene-1,3-disulfonamide
isoenzyme hCA VA
0.000243
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0039
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0052
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0055
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0066
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0085
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0159
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0185
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0314
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0495
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0694
7-(2-phenylethoxy)-2H-chromen-2-one
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000224
7-(benzyloxy)-2H-chromen-2-one
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0017
7-(benzyloxy)-2H-chromen-2-one
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.002
7-(benzyloxy)-2H-chromen-2-one
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0076
7-(benzyloxy)-2H-chromen-2-one
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0083
7-(benzyloxy)-2H-chromen-2-one
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0097
7-(benzyloxy)-2H-chromen-2-one
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0118
7-(benzyloxy)-2H-chromen-2-one
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0192
7-(benzyloxy)-2H-chromen-2-one
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0269
7-(benzyloxy)-2H-chromen-2-one
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0402
7-(benzyloxy)-2H-chromen-2-one
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0651
7-(benzyloxy)-2H-chromen-2-one
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000213
7-butoxy-2H-chromen-2-one
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0043
7-butoxy-2H-chromen-2-one
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0045
7-butoxy-2H-chromen-2-one
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0085
7-butoxy-2H-chromen-2-one
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.009
7-butoxy-2H-chromen-2-one
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.015
7-butoxy-2H-chromen-2-one
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0249
7-butoxy-2H-chromen-2-one
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0268
7-butoxy-2H-chromen-2-one
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.037
7-butoxy-2H-chromen-2-one
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0503
7-butoxy-2H-chromen-2-one
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0764
7-butoxy-2H-chromen-2-one
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0016
7-ethoxy-2H-chromen-2-one
isoform CA IX, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0047
7-ethoxy-2H-chromen-2-one
isoform CA XII, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0047
7-ethoxy-2H-chromen-2-one
isoform CA XIV, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0058
7-ethoxy-2H-chromen-2-one
isoform CA VI, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0072
7-ethoxy-2H-chromen-2-one
isoform CA VII, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0073
7-ethoxy-2H-chromen-2-one
isoform CA VA, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0124
7-ethoxy-2H-chromen-2-one
isoform CA II, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0227
7-ethoxy-2H-chromen-2-one
isoform CA IV, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.029
7-ethoxy-2H-chromen-2-one
Ki above 0.5 mM, isoform CA III, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0314
7-ethoxy-2H-chromen-2-one
isoform CA I, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0609
7-ethoxy-2H-chromen-2-one
isoform CA VB, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0000332
7-ethoxy-8-propanoyl-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000467
7-ethoxy-8-propanoyl-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.000093
7-hydroxy-1-methoxy-3-methyl-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
isoform CA VA
0.000103
7-hydroxy-1-methoxy-3-methyl-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
isoform CA VB
0.0084
7-hydroxy-1-methoxy-3-methyl-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
isoform CA II
0.201
7-hydroxy-1-methoxy-3-methyl-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
isoform CA I
0.000094
7-hydroxy-3-(hydroxymethyl)-1-methoxy-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
isoform CA VA
0.000102
7-hydroxy-3-(hydroxymethyl)-1-methoxy-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
isoform CA VB
0.0092
7-hydroxy-3-(hydroxymethyl)-1-methoxy-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
isoform CA II
0.374
7-hydroxy-3-(hydroxymethyl)-1-methoxy-9-oxo-9,9a-dihydro-4aH-xanthene-8-carboxylic acid
-
isoform CA I
0.0000582
7-hydroxy-8-propanoyl-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0000617
7-hydroxy-8-propanoyl-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.000099
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.00372
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0094
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0723
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0823
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
IC50 above 0.5 mM, isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
IC50 above 0.5 mM, isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
IC50 above 0.5 mM, isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
IC50 above 0.5 mM, isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
IC50 above 0.5 mM, isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
7-methoxy-2-oxo-2H-chromene-4-carboxylic acid
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000066
7-methoxy-2H-chromen-2-one
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0059
7-methoxy-2H-chromen-2-one
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0078
7-methoxy-2H-chromen-2-one
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0091
7-methoxy-2H-chromen-2-one
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0097
7-methoxy-2H-chromen-2-one
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0486
7-methoxy-2H-chromen-2-one
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0612
7-methoxy-2H-chromen-2-one
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.161
7-methoxy-2H-chromen-2-one
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.1674
7-methoxy-2H-chromen-2-one
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
7-methoxy-2H-chromen-2-one
IC50 above 0.5 mM, isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.5
7-methoxy-2H-chromen-2-one
IC50 above 0.5 mM, isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0000263
7-methoxy-8-propanoyl-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000378
7-methoxy-8-propanoyl-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0033
7-propoxy-2H-chromen-2-one
isoform CA IX, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.005
7-propoxy-2H-chromen-2-one
isoform CA XIV, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0077
7-propoxy-2H-chromen-2-one
isoform CA VII, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0081
7-propoxy-2H-chromen-2-one
isoform CA VA, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0086
7-propoxy-2H-chromen-2-one
isoform CA XII, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0231
7-propoxy-2H-chromen-2-one
isoform CA I, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0246
7-propoxy-2H-chromen-2-one
isoform CA IV, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0374
7-propoxy-2H-chromen-2-one
isoform CA VI, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0386
7-propoxy-2H-chromen-2-one
Ki above 0.5 mM, isoform CA III, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0717
7-propoxy-2H-chromen-2-one
isoform CA VB, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.145
7-propoxy-2H-chromen-2-one
isoform CA II, in 20m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0000224
8-acetyl-7-(benzyloxy)-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000723
8-acetyl-7-(benzyloxy)-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0000088
8-acetyl-7-butoxy-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000612
8-acetyl-7-butoxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.000001
8-acetyl-7-ethoxy-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000708
8-acetyl-7-ethoxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0000619
8-acetyl-7-hydroxy-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.000073
8-acetyl-7-hydroxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0000609
8-acetyl-7-methoxy-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000783
8-acetyl-7-methoxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.00000098
8-acetyl-7-propoxy-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000567
8-acetyl-7-propoxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.001
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0013
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0058
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0061
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0065
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0074
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0086
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0094
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0171
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0256
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0301
8-methoxy-2-oxo-2H-chromene-3-carboxylic acid
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0000384
8-propanoyl-7-propoxy-2H-chromen-2-one
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0000502
8-propanoyl-7-propoxy-2H-chromen-2-one
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0000025
acetazolamide
isoenzyme hCA VII
0.0000025
acetazolamide
isozyme CA VII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000005
acetazolamide
recombinant enzyme, pH and temperature not specified in the publication
0.0000057
acetazolamide
pH 7.5, catalytic domain of cloned isoenzyme
0.0000057
acetazolamide
isoenzyme hCA XII
0.0000057
acetazolamide
isozyme CA XII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0000057
acetazolamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000057
acetazolamide
pH and temperature not specified in the publication
0.000009
acetazolamide
recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Zn2+
0.0000105
acetazolamide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.000011
acetazolamide
isoenzyme hCA VI
0.000011
acetazolamide
isozyme CA VI, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000012
acetazolamide
isoenzyme hCA II
0.000012
acetazolamide
isozyme CA II, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000012
acetazolamide
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000012
acetazolamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000012
acetazolamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000012
acetazolamide
pH and temperature not specified in the publication
0.000016
acetazolamide
recombinant extracellular domain of CA IX expressed in Sf9 cells, in the absence of Zn2+
0.000016
acetazolamide
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.000024
acetazolamide
recombinant CA IX catalytic domain expressed in Sf9 cells, in the absence of Zn2+
0.000025
acetazolamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000025
acetazolamide
isoenzyme hCA IX
0.000025
acetazolamide
isozyme CA IX, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000025
acetazolamide
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000025
acetazolamide
recombinant CA IX catalytic domain expressed in Escherichia coli
0.000025
acetazolamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000025
acetazolamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000025
acetazolamide
pH and temperature not specified in the publication
0.000026
acetazolamide
-
pH 7.4, 30°C, inhibition of CO2 hydration activity
0.000041
acetazolamide
pH 7.5, full-length recombinant enzyme
0.000041
acetazolamide
isoenzyme hCA XIV
0.000041
acetazolamide
isozyme CA XIV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000041
acetazolamide
recombinant extracellular domain of CA IX expressed in Sf9 cells, in the presence of 0.05 mM Mn2+
0.000041
acetazolamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000041
acetazolamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00005
acetazolamide
-
pH 9.0, 30°C, inhibition of esterase activity with 4-nitrophenyl acetate
0.000054
acetazolamide
isoenzyme hCA VB
0.000054
acetazolamide
isozyme CA VB, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000055
acetazolamide
recombinant extracellular domain of CA IX expressed in Sf9 cells, in the presence of 0.05 mM Mg2+
0.000056
acetazolamide
recombinant extracellular domain of CA IX expressed in Sf9 cells, in the presence of 0.05 mM Co2+
0.000063
acetazolamide
isoenzyme hCA VA
0.000063
acetazolamide
isozyme CA VA, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000063
acetazolamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000063
acetazolamide
isozyme bsCAI, pH 8.3, temperature not specified in the publication
0.000063
acetazolamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.000074
acetazolamide
isoenzyme hCA IV
0.000074
acetazolamide
isozyme CA IV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0000789
acetazolamide
pH 8.3, 20°C, recombinant His-tagged enzyme
0.000082
acetazolamide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.000104
acetazolamide
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.000132
acetazolamide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.00017
acetazolamide
pH 7.5, 22°C, truncated form PfCA1, CO2 hydration reaction
0.000214
acetazolamide
pH 8.3, 22°C, recombinant His-tagged enzyme
0.00025
acetazolamide
isoenzyme hCA I
0.00025
acetazolamide
isozyme CA I, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00025
acetazolamide
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00025
acetazolamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00025
acetazolamide
pH and temperature not specified in the publication
0.00025
acetazolamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.000303
acetazolamide
isozyme bsCAII, pH 8.3, temperature not specified in the publication
0.00031
acetazolamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000361
acetazolamide
CO2 hydration, pH 8.3, 22°C, recombinant enzyme
0.000366
acetazolamide
pH 7.5, 22°C, long enzyme form PfCAdom, CO2 hydration reaction
0.00038
acetazolamide
CO2 hydration, pH 8.3, 22°C, native enzyme
0.000481
acetazolamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00143
acetazolamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.002325
acetazolamide
recombinant extracellular domain of CA IX expressed in Sf9 cells, in the presence of 0.05 mM Zn2+
0.012
acetazolamide
-
20°C, pH not specified in the publication
0.2
acetazolamide
isozyme CA III, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.3
acetazolamide
isoenzyme hCA III
0.00000064
azetazolamide
-
pH not specified in the publication, 4°C, assay using the delta pH method
4.9
azide
Co(II)-substituted enzyme, pH and temperature not specified in the publication
5.8
azide
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
4.7
B4O72-
pH 8.3, 22°C, inhibition of CO2 hydration activity
8
B4O72-
pH 8.3, 20°C, inhibition of CO2 hydration activity
4.003
benzene-1,2-diol
pH 7.4, temperature not specified in the publication
0.795
benzene-1,3-diol
pH 7.4, temperature not specified in the publication
0.00514
benzene-1,3-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.005885
benzene-1,3-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA3
0.0000204
benzolamide
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.000338
benzolamide
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.00081
benzolamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0102
Benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate
pH 7.5, 22°C
4.1
Benzyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate
pH 7.5, 22°C
0.00319
benzyl (2E)-3-(3-hydroperoxy-4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00451
benzyl (2E)-3-(3-hydroperoxy-4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00705
benzyl (2E)-3-(3-hydroperoxy-4-hydroxyphenyl)prop-2-enoate
pH 8.3, 25°C, recombinant enzyme
0.00184
benzyl 4-coumarate
pH 8.3, 25°C, recombinant enzyme
0.00378
benzyl 4-coumarate
pH 8.3, 25°C, recombinant enzyme
0.00504
benzyl 4-coumarate
pH 8.3, 25°C, recombinant enzyme
0.78
bicarbonate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.33
bisulfite
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.96
Br-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
8.7
Br-
pH 8.3, 20°C, inhibition of CO2 hydration activity
22.2
Br-
20°C, pH not specified in the publication, Co2+-substituted enzyme
22.2
Br-
Co(II)-substituted enzyme, pH and temperature not specified in the publication
160
Br-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
160
Br-
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.0000028
brinzolamide
isoenzyme hCA VII catalytic domain
0.000003
brinzolamide
isoenzyme hCA II
0.000003
brinzolamide
isoenzyme hCA XII catalytic domain
0.000003
brinzolamide
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000009
brinzolamide
isoenzyme hCA VI catalytic domain
0.000024
brinzolamide
isoenzyme hCA XIV catalytic domain catalytic domain
0.00003
brinzolamide
isoenzyme hCA VB catalytic domain
0.000037
brinzolamide
isoenzyme hCA IX catalytic domain
0.000047
brinzolamide
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000482
brinzolamide
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.00005
brinzolamide
isoenzyme hCA VA catalytic domain
0.000201
brinzolamide
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.00045
brinzolamide
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000839
brinzolamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00395
brinzolamide
isoenzyme hCA IV catalytic domain
0.045
brinzolamide
isoenzyme hCA I
0.11
brinzolamide
isoenzyme hCA III
0.0108
bromide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.009
Carbonate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
0.6
Carbonate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.76
Carbonate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
6.7
Carbonate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.0099
catechol
pH 7.4, temperature not specified in the publication
0.000016
celecoxib
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.000018
celecoxib
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.000021
celecoxib
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.0000342
celecoxib
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.00014
celecoxib
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.000217
celecoxib
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA36
0.00101
celecoxib
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00776
celecoxib
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.00838
celecoxib
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.01035
celecoxib
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0385
celecoxib
-
20°C, pH not specified in the publication
0.05
celecoxib
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
7.7
CF3SO3-
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.85
chloride
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.92
chloride
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.0000028
Chlorthalidone
isozyme CA VII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0000045
Chlorthalidone
isozyme CA XII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000009
Chlorthalidone
isozyme CA VB, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000023
Chlorthalidone
isozyme CA IX, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000138
Chlorthalidone
isozyme CA II, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000348
Chlorthalidone
isozyme CA I, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000917
Chlorthalidone
isozyme CA VA, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.001357
Chlorthalidone
isozyme CA VI, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00413
Chlorthalidone
isozyme CA XIV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.196
Chlorthalidone
isozyme CA IV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
1.11
Chlorthalidone
isozyme CA III, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.53
Cl-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
0.68
CN-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.86
CN-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
5.9
CN-
pH 8.3, 20°C, inhibition of CO2 hydration activity
51.5
CN-
20°C, pH not specified in the publication, Co2+-substituted enzyme
0.0024
CNO-
-
pH not specified in the publication, 4°C, assay using the delta pH method
0.09
CNO-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.69
CNO-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
1.7
CNO-
pH 8.3, 20°C, inhibition of CO2 hydration activity
4.7
CNO-
20°C, pH not specified in the publication, Co2+-substituted enzyme
0.009
CO32-
20°C, pH not specified in the publication, Co2+-substituted enzyme
0.24
CO32-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
1.4
CO32-
pH 8.3, 22°C, inhibition of CO2 hydration activity
2.5
CO32-
pH 8.3, 20°C, inhibition of CO2 hydration activity
6.7
CO32-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.0001
coumarin
-
inhibition of isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.0001
coumarin
-
inhibition of isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.0031
coumarin
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0092
coumarin
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
3.8
CS32-
pH 8.3, 22°C, inhibition of CO2 hydration activity
34.6
CS32-
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.0004
Cu2+
-
pH not specified in the publication, 4°C, assay using the delta pH method
0.0309
Cu2+
-
pH not specified in the publication, 4°C, assay using the delta pH method
0.09
Cyanate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
4.7
Cyanate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
31.7
Cyanate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.68
cyanide
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
13.56
cyanide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
16.8
cyanide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
51.5
cyanide
Co(II)-substituted enzyme, pH and temperature not specified in the publication
0.000038
dichlorophenamide
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000038
dichlorophenamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00005
dichlorophenamide
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00005
dichlorophenamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00005
dichlorophenamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000345
dichlorophenamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000431
dichlorophenamide
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.000611
dichlorophenamide
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.0012
dichlorophenamide
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0012
dichlorophenamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0012
dichlorophenamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.0000035
dorzolamide
isoenzyme hCA VII
0.0000035
dorzolamide
isoenzyme hCA XII
0.000009
dorzolamide
isoenzyme hCA II
0.000009
dorzolamide
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.00001
dorzolamide
isoenzyme hCA VI
0.0000181
dorzolamide
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.000027
dorzolamide
isoenzyme hCA XIV catalytic domain
0.000033
dorzolamide
isoenzyme hCA VB
0.000042
dorzolamide
isoenzyme hCA VA
0.000052
dorzolamide
isoenzyme hCA IX
0.000052
dorzolamide
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000137
dorzolamide
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.00041
dorzolamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.0005
dorzolamide
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000744
dorzolamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00171
dorzolamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0085
dorzolamide
isoenzyme hCA IV
0.0307
dorzolamide
-
20°C, pH not specified in the publication
0.05
dorzolamide
isoenzyme hCA I
0.77
dorzolamide
isoenzyme hCA III
0.58
Et2NCS2-
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.96
Et2NCS2-
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.000008
ethoxazolamide
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000025
ethoxazolamide
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000034
ethoxazolamide
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.0000008
ethoxzolamide
isoenzyme hCA VII
0.0000008
ethoxzolamide
isoenzyme hCA VII
0.0000008
ethoxzolamide
isozyme CA VII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000001
ethoxzolamide
Ki less than 0.000001 mM wild type carbonic anhydrase II
0.000008
ethoxzolamide
isoenzyme hCA II
0.000008
ethoxzolamide
isozyme CA II, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000008
ethoxzolamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000019
ethoxzolamide
isoenzyme hCA VB
0.000019
ethoxzolamide
isoenzyme hCA VB
0.000019
ethoxzolamide
isozyme CA VB, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000022
ethoxzolamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000022
ethoxzolamide
isoenzyme hCA XII
0.000022
ethoxzolamide
isoenzyme hCA XII
0.000022
ethoxzolamide
isozyme CA XII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000022
ethoxzolamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000025
ethoxzolamide
pH 7.5, full-length recombinant enzyme
0.000025
ethoxzolamide
isoenzyme hCA I
0.000025
ethoxzolamide
isoenzyme hCA VA
0.000025
ethoxzolamide
isoenzyme hCA VA
0.000025
ethoxzolamide
isoenzyme hCA XIV
0.000025
ethoxzolamide
isoenzyme hCA XIV catalytic domain
0.000025
ethoxzolamide
isozyme CA I, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000025
ethoxzolamide
isozyme CA VA, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000025
ethoxzolamide
isozyme CA XIV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000025
ethoxzolamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000025
ethoxzolamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000034
ethoxzolamide
isoenzyme hCA IX
0.000034
ethoxzolamide
isoenzyme hCA IX
0.000034
ethoxzolamide
isozyme CA IX, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000034
ethoxzolamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000394
ethoxzolamide
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.000043
ethoxzolamide
isoenzyme hCA VI
0.000043
ethoxzolamide
isoenzyme hCA VI
0.000043
ethoxzolamide
isozyme CA VI, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00005
ethoxzolamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00008
ethoxzolamide
isoenzyme hCA II
0.000093
ethoxzolamide
isoenzyme hCA IV
0.000093
ethoxzolamide
isoenzyme hCA IV
0.000093
ethoxzolamide
isozyme CA IV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0002
ethoxzolamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00025
ethoxzolamide
isoenzyme hCA I
0.000594
ethoxzolamide
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.00074
ethoxzolamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00103
ethoxzolamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.005
ethoxzolamide
isoenzyme hCA III
0.00535
ethoxzolamide
-
20°C, pH not specified in the publication
0.011
ethoxzolamide
isozyme CA III, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
1.1
ethoxzolamide
isoenzyme hCA III
0.000045
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000047
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000048
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0015
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0029
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.003
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0033
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0046
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0084
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0096
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0505
ethyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0024
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0057
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0065
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.008
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0088
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0091
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0095
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0096
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0203
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0314
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.042
ethyl 7-methoxy-2-oxo-2H-chromene-3-carboxylate
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.92
F-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
0.86
fluoride
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
2.85
fluoride
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
4.3
FSO3-
pH 8.3, 22°C, inhibition of CO2 hydration activity
7.7
FSO3-
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.000052
Furosemide
isoenzyme hCA XIV
0.000062
Furosemide
isoenzyme hCA I
0.000065
Furosemide
isoenzyme hCA II
0.000245
Furosemide
isoenzyme hCA VI
0.000261
Furosemide
isoenzyme hCA XII
0.000322
Furosemide
isoenzyme hCA VB
0.00042
Furosemide
isoenzyme hCA IX
0.000499
Furosemide
isoenzyme hCA VA
0.000513
Furosemide
isoenzyme hCA VII
0.000564
Furosemide
isoenzyme hCA IV
0.0057
H2NSO2NH2
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
0.008
H2NSO2NH2
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.082
H2NSO2NH2
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.0085
H2NSO3H
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
0.037
H2NSO3H
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.091
H2NSO3H
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.1
HCO3-
20°C, pH not specified in the publication, Co2+-substituted enzyme
1.7
HCO3-
pH 8.3, 22°C, inhibition of CO2 hydration activity
6.2
HCO3-
pH 8.3, 20°C, inhibition of CO2 hydration activity
7.81
HCO3-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
42
HCO3-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
44.9
HCO3-
-
20°C, pH not specified in the publication
0.000075
heptane-1,7-diyl disulfamate
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.000193
heptane-1,7-diyl disulfamate
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.0000003
homosulfanilamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000103
homosulfanilamide
pH 7.5, catalytic domain of cloned isoenzyme
0.0032
homosulfanilamide
pH 7.5, full-length recombinant enzyme
0.05
HS-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
2
HS-
20°C, pH not specified in the publication, Co2+-substituted enzyme
3.94
HS-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
8.4
HS-
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.43
HSO3-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
1.8
HSO3-
20°C, pH not specified in the publication, Co2+-substituted enzyme
11.7
HSO3-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
24.1
HSO3-
pH 8.3, 20°C, inhibition of CO2 hydration activity
37.5
HSO3-
pH 8.3, 22°C, inhibition of CO2 hydration activity
45.1
HSO3-
-
20°C, pH not specified in the publication
0.00029
hydrochlorothiazide
isoenzyme hCA II
0.000328
hydrochlorothiazide
isoenzyme hCA I
0.000355
hydrochlorothiazide
isoenzyme hCA XII
0.000367
hydrochlorothiazide
isoenzyme hCA IX
0.000427
hydrochlorothiazide
isoenzyme hCA IV
0.000603
hydrochlorothiazide
isoenzyme hCA VB
0.003655
hydrochlorothiazide
isoenzyme hCA VI
0.004105
hydrochlorothiazide
isoenzyme hCA XIV
0.004225
hydrochlorothiazide
isoenzyme hCA VA
0.00501
hydrochlorothiazide
isoenzyme hCA VII
0.62
hydrogen carbonate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.75
hydrogen carbonate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.05
hydrogen sulfide
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.33
hydrogen sulfide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.37
hydrogen sulfide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.6
hydrogen sulfide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
2
hydrogen sulfide
Co(II)-substituted enzyme, pH and temperature not specified in the publication
0.54
hydrogen sulfite
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.71
hydrogen sulfite
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
1.8
hydrogen sulfite
Co(II)-substituted enzyme, pH and temperature not specified in the publication
11.7
hydrogen sulfite
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.1
hydrogencarbonate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
42
hydrogencarbonate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
5.3
I-
20°C, pH not specified in the publication, Co2+-substituted enzyme
5.3
I-
Co(II)-substituted enzyme, pH and temperature not specified in the publication
33
I-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
160
I-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
160
I-
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
0.00000023
indapamide
isozyme CA VII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00001
indapamide
isozyme CA XII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000036
indapamide
isozyme CA IX, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000138
indapamide
isozyme CA I, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000213
indapamide
isozyme CA IV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000274
indapamide
isozyme CA VB, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00089
indapamide
isozyme CA VA, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.001606
indapamide
isozyme CA VI, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00252
indapamide
isozyme CA II, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00495
indapamide
isozyme CA XIV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0000034
indisulam
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000015
indisulam
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000024
indisulam
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000031
indisulam
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000097
indisulam
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.000104
indisulam
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000163
indisulam
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.00784
indisulam
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.0103
Iodide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
1.01
isocyanide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.0004585
Isoorotic acid
pH 7.4, temperature not specified in the publication
1.432
Isoorotic acid
pH 7.4, temperature not specified in the publication
0.0000021
methazolamide
isozyme CA VII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0000034
methazolamide
isozyme CA XII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.0000034
methazolamide
-
isoform CA XII, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00001
methazolamide
isozyme CA VI, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000014
methazolamide
isozyme CA II, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000014
methazolamide
-
isozyme CA II, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000014
methazolamide
-
isoform CA II, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.0000212
methazolamide
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.000027
methazolamide
isozyme CA IX, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000027
methazolamide
-
isozyme CA IX, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000027
methazolamide
-
isoform CA IX, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000043
methazolamide
isozyme CA XIV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000043
methazolamide
-
isoform CA XIV, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.00005
methazolamide
isozyme CA I, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00005
methazolamide
-
isozyme CA I, in 10 mM HEPES (pH 7.5), 0.1 M NaClO4, at 20°C
0.000062
methazolamide
isozyme CA VB, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000065
methazolamide
isozyme CA VA, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.00014
methazolamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00017
methazolamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.000198
methazolamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA25
0.000562
methazolamide
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.000655
methazolamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00078
methazolamide
-
isoform CA I, in 10 mM HEPES (pH 7.5), 0.1 M Na2SO4, at 22°C
0.000781
methazolamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.0062
methazolamide
isozyme CA IV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.032
methazolamide
-
20°C, pH not specified in the publication
0.7
methazolamide
isozyme CA III, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4
0.000032
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA II, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000045
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA IX, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000098
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA I, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0056
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA XII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0065
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA IV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0071
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA VB, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0073
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA VII, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0073
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA XIV, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0084
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA VA, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0089
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA III, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.0095
methyl 6-(hydroxymethyl)-2-oxo-2H-chromene-3-carboxylate
isoform CA VI, in 20 m M HEPES (pH 7.5), and 20 mM Na2SO4, at 22°C
0.000015
N,N'-biphosphoryl-4,5-dichloro-1,3-benzenesulfonamide
-
pH 7.4, 25°C, hCA II
0.000052
N,N'-biphosphoryl-4,5-dichloro-1,3-benzenesulfonamide
-
pH 7.4, 25°C, hCA I
0.000074
N-(1-(2-hydroxyphenylamino)-3-methyl-1-oxobutan-2-ylcarbamothioyl)benzamide
pH 8.3, 22°C
0.000481
N-(1-(2-hydroxyphenylamino)-3-methyl-1-oxobutan-2-ylcarbamothioyl)benzamide
above, pH 8.3, 22°C
1
N-(1-(2-hydroxyphenylamino)-3-methyl-1-oxobutan-2-ylcarbamothioyl)benzamide
above, pH 8.3, 22°C
0.000068
N-(1-(2-hydroxyphenylamino)-4-methyl-1-oxopentan-2-ylcarbamothioyl) benzamide
pH 8.3, 22°C
0.00049
N-(1-(2-hydroxyphenylamino)-4-methyl-1-oxopentan-2-ylcarbamothioyl) benzamide
above, pH 8.3, 22°C
1
N-(1-(2-hydroxyphenylamino)-4-methyl-1-oxopentan-2-ylcarbamothioyl) benzamide
above, pH 8.3, 22°C
0.000007
N-(2-fluoro-4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAVII, pH 7.5, temperature not specified in the publication
0.000161
N-(2-fluoro-4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAI, pH 7.5, temperature not specified in the publication
0.00039
N-(2-fluoro-4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAII, pH 7.5, temperature not specified in the publication
0.000437
N-(2-fluoro-4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAXIII, pH 7.5, temperature not specified in the publication
0.12
N-(2-fluoro-4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAIII, pH 7.5, temperature not specified in the publication
0.000008
N-(3-chloro-1H-indol-7-yl)benzene-1,4-disulfonamide
-
pH 7.5, 20°C
0.0000845
N-(3-chloro-1H-indol-7-yl)benzene-1,4-disulfonamide
-
pH 7.5, 20°C
0.000113
N-(3-chloro-1H-indol-7-yl)benzene-1,4-disulfonamide
-
pH 8.3, 20°C
0.000316
N-(3-chloro-1H-indol-7-yl)benzene-1,4-disulfonamide
-
pH 7.5, 20°C
0.000423
N-(3-chloro-1H-indol-7-yl)benzene-1,4-disulfonamide
-
pH 7.5, 20°C
0.0000062
N-(4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAVII, pH 7.5, temperature not specified in the publication
0.00005
N-(4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAII, pH 7.5, temperature not specified in the publication
0.000061
N-(4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAI, pH 7.5, temperature not specified in the publication
0.000125
N-(4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAXIII, pH 7.5, temperature not specified in the publication
0.08
N-(4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide
-
inhibition of CO2 hydration by isozyme hCAIII, pH 7.5, temperature not specified in the publication
0.0000092
N-(4-sulfamoylphenyl)-beta-D-galactopyranosylamine
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.0000101
N-(4-sulfamoylphenyl)-beta-D-galactopyranosylamine
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.0000089
N-(4-sulfamoylphenyl)-beta-D-idopyranosylamine
pH 8.3, temperature not specified in the publication, isozyme bsCA I
0.0000146
N-(4-sulfamoylphenyl)-beta-D-idopyranosylamine
pH 8.3, temperature not specified in the publication, isozyme bsCA II
0.00003
N-(4-[(E)-[(aminosulfonyl)imino]methyl]phenyl)acetamide
-
pH 7.4, 25°C, isozyme hCA II
0.007
N-(4-[(E)-[(aminosulfonyl)imino]methyl]phenyl)acetamide
-
pH 7.4, 25°C, isozyme hCA I
0.01
N-(4-[(E)-[(aminosulfonyl)imino]methyl]phenyl)acetamide
-
pH 7.4, 25°C, isozyme bCA IV
0.001
N-(4-[[(aminosulfonyl)amino]sulfonyl]phenyl)acetamide
-
pH 7.4, 25°C, isozyme hCA I
0.0011
N-(4-[[(aminosulfonyl)amino]sulfonyl]phenyl)acetamide
-
pH 7.4, 25°C, isozyme hCA II
0.002
N-(4-[[(aminosulfonyl)amino]sulfonyl]phenyl)acetamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0000057
N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)acetamide
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.0000068
N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)acetamide
-
pH 7.5, 20°C
0.000012
N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)acetamide
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.000025
N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)acetamide
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.0000024
N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)furan-2-carboxamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000013
N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)furan-2-carboxamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000023
N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)furan-2-carboxamide
pH 7.5, full-length recombinant enzyme
0.000768
N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)furan-2-carboxamide
-
pH 7.5, 20°C
0.000074
N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.000125
N-(5-sulfanyl-1,3,4-thiadiazol-2-yl)hydrazinecarboxamide
-
pH 7.5, 20°C
0.01
N-(aminosulfonyl)-1,1,1-trichloromethanesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.02
N-(aminosulfonyl)-1,1,1-trichloromethanesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.07
N-(aminosulfonyl)-1,1,1-trichloromethanesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.01
N-(aminosulfonyl)-1,1,1-trifluoromethanesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.02
N-(aminosulfonyl)-1,1,1-trifluoromethanesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.07
N-(aminosulfonyl)-1,1,1-trifluoromethanesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.002
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,4-nonafluorobutane-1-sulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.01
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,4-nonafluorobutane-1-sulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.04
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,4-nonafluorobutane-1-sulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0011
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.008
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.03
N-(aminosulfonyl)-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.005
N-(aminosulfonyl)-1-(7,7-dimethylbicyclo[2.2.1]hept-1-yl)methanesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.007
N-(aminosulfonyl)-1-(7,7-dimethylbicyclo[2.2.1]hept-1-yl)methanesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.009
N-(aminosulfonyl)-1-(7,7-dimethylbicyclo[2.2.1]hept-1-yl)methanesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.03
N-(aminosulfonyl)-1-phenylmethanesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.00005
N-(aminosulfonyl)-2,3,4,5,6-pentafluorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.0012
N-(aminosulfonyl)-2,3,4,5,6-pentafluorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.0018
N-(aminosulfonyl)-2,3,4,5,6-pentafluorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.001
N-(aminosulfonyl)-2,4,6-triisopropylbenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.0012
N-(aminosulfonyl)-2,4,6-triisopropylbenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.0035
N-(aminosulfonyl)-2,4,6-triisopropylbenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0012
N-(aminosulfonyl)-2,4,6-tripropylbenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.0017
N-(aminosulfonyl)-2,4,6-tripropylbenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.0039
N-(aminosulfonyl)-2,4,6-tripropylbenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0009
N-(aminosulfonyl)-2,5-dichlorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.0015
N-(aminosulfonyl)-2,5-dichlorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.0032
N-(aminosulfonyl)-2,5-dichlorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0017
N-(aminosulfonyl)-2-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.002
N-(aminosulfonyl)-2-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.0008
N-(aminosulfonyl)-3,5-dichloro-2-hydroxybenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.0009
N-(aminosulfonyl)-3,5-dichloro-2-hydroxybenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.0021
N-(aminosulfonyl)-3,5-dichloro-2-hydroxybenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0009
N-(aminosulfonyl)-3-(trifluoromethyl)benzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.0016
N-(aminosulfonyl)-3-(trifluoromethyl)benzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.0026
N-(aminosulfonyl)-3-(trifluoromethyl)benzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0011
N-(aminosulfonyl)-3-chloro-4-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.002
N-(aminosulfonyl)-3-chloro-4-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.003
N-(aminosulfonyl)-3-chloro-4-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0016
N-(aminosulfonyl)-3-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.0019
N-(aminosulfonyl)-3-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.03
N-(aminosulfonyl)-4-chlorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.03
N-(aminosulfonyl)-4-fluorobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.004
N-(aminosulfonyl)-4-methoxybenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.01
N-(aminosulfonyl)-4-methoxybenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.02
N-(aminosulfonyl)-4-methylbenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.0014
N-(aminosulfonyl)-4-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.0015
N-(aminosulfonyl)-4-nitrobenzenesulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.003
N-(aminosulfonyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
pH 7.4, 25°C, isozyme hCA I
0.01
N-(aminosulfonyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
pH 7.4, 25°C, isozyme bCA IV
0.01
N-(aminosulfonyl)-5-(dimethylamino)naphthalene-1-sulfonamide
-
pH 7.4, 25°C, isozyme hCA II
0.000002
N-phosphoryl-6-nitro-benzothiazole-2-sulfonamide
-
pH 7.4, 25°C, hCA II
0.000023
N-salicylidene-sulfanilic acid amide cobalt acetate complex
-
pH 7.4, 25°C, isozyme hCA II
0.000073
N-salicylidene-sulfanilic acid amide cobalt acetate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00033
N-salicylidene-sulfanilic acid amide cobalt acetate complex
-
pH 7.4, 25°C, isozyme hCA I
0.000024
N-salicylidene-sulfanilic acid amide cobalt chloride complex
-
pH 7.4, 25°C, isozyme hCA II
0.000078
N-salicylidene-sulfanilic acid amide cobalt chloride complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00033
N-salicylidene-sulfanilic acid amide cobalt chloride complex
-
pH 7.4, 25°C, isozyme hCA I
0.000025
N-salicylidene-sulfanilic acid amide cobalt nitrate complex
-
pH 7.4, 25°C, isozyme hCA II
0.000073
N-salicylidene-sulfanilic acid amide cobalt nitrate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00032
N-salicylidene-sulfanilic acid amide cobalt nitrate complex
-
pH 7.4, 25°C, isozyme hCA I
0.000022
N-salicylidene-sulfanilic acid amide cobalt sulfate complex
-
pH 7.4, 25°C, isozyme hCA II
0.000072
N-salicylidene-sulfanilic acid amide cobalt sulfate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00035
N-salicylidene-sulfanilic acid amide cobalt sulfate complex
-
pH 7.4, 25°C, isozyme hCA I
0.000013
N-salicylidene-sulfanilic acid amide copper chloride complex
-
pH 7.4, 25°C, isozyme hCA II
0.000083
N-salicylidene-sulfanilic acid amide copper chloride complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00021
N-salicylidene-sulfanilic acid amide copper chloride complex
-
pH 7.4, 25°C, isozyme hCA I
0.000015
N-salicylidene-sulfanilic acid amide copper nitrate complex
-
pH 7.4, 25°C, isozyme hCA II
0.00008
N-salicylidene-sulfanilic acid amide copper nitrate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00024
N-salicylidene-sulfanilic acid amide copper nitrate complex
-
pH 7.4, 25°C, isozyme hCA I
0.000037
N-salicylidene-sulfanilic acid amide nickel acetate complex
-
pH 7.4, 25°C, isozyme hCA II
0.000108
N-salicylidene-sulfanilic acid amide nickel acetate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00055
N-salicylidene-sulfanilic acid amide nickel acetate complex
-
pH 7.4, 25°C, isozyme hCA I
0.000039
N-salicylidene-sulfanilic acid amide nickel chloride complex
-
pH 7.4, 25°C, isozyme hCA II
0.000105
N-salicylidene-sulfanilic acid amide nickel chloride complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00054
N-salicylidene-sulfanilic acid amide nickel chloride complex
-
pH 7.4, 25°C, isozyme hCA I
0.000039
N-salicylidene-sulfanilic acid amide nickel nitrate complex
-
pH 7.4, 25°C, isozyme hCA II
0.000102
N-salicylidene-sulfanilic acid amide nickel nitrate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00056
N-salicylidene-sulfanilic acid amide nickel nitrate complex
-
pH 7.4, 25°C, isozyme hCA I
0.000036
N-salicylidene-sulfanilic acid amide nickel sulfate complex
-
pH 7.4, 25°C, isozyme hCA II
0.000106
N-salicylidene-sulfanilic acid amide nickel sulfate complex
-
pH 7.4, 25°C, isozyme bCA IV
0.00055
N-salicylidene-sulfanilic acid amide nickel sulfate complex
-
pH 7.4, 25°C, isozyme hCA I
0.00094
N-sulfamoyl-beta-D-galactopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.00823
N-sulfamoyl-beta-D-galactopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0485
N-sulfamoyl-beta-D-galactopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.0658
N-sulfamoyl-beta-D-galactopyranosylamine
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.00197
N-sulfamoyl-beta-D-glucopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.00468
N-sulfamoyl-beta-D-glucopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.00647
N-sulfamoyl-beta-D-glucopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.0754
N-sulfamoyl-beta-D-glucopyranosylamine
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.00179
N-sulfamoyl-beta-D-mannopyranosylamine
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.00544
N-sulfamoyl-beta-D-mannopyranosylamine
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.0212
N-sulfamoyl-beta-D-mannopyranosylamine
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.0919
N-sulfamoyl-beta-D-mannopyranosylamine
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.00007
N-[(1E)-(1-methyl-1H-pyrrol-2-yl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA II
0.01
N-[(1E)-(1-methyl-1H-pyrrol-2-yl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme bCA IV
0.01
N-[(1E)-(1-methyl-1H-pyrrol-2-yl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA I
0.00002
N-[(1E)-(3,4,5-trimethoxyphenyl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA II
0.009
N-[(1E)-(3,4,5-trimethoxyphenyl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA I
0.01
N-[(1E)-(3,4,5-trimethoxyphenyl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme bCA IV
0.0014
N-[(1E)-(3-nitrophenyl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA II
0.00004
N-[(1E)-(4-methoxyphenyl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA II
0.00005
N-[(1E)-(4-methylphenyl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA II
0.0015
N-[(1E)-(4-nitrophenyl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA II
0.00004
N-[(1E)-(5-methylthien-2-yl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA II
0.009
N-[(1E)-(5-methylthien-2-yl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA I
0.01
N-[(1E)-(5-methylthien-2-yl)methylene]sulfamide
-
pH 7.4, 25°C, isozyme bCA IV
0.00002
N-[(1E)-[4-(dimethylamino)phenyl]methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA II
0.008
N-[(1E)-[4-(dimethylamino)phenyl]methylene]sulfamide
-
pH 7.4, 25°C, isozyme bCA IV
0.008
N-[(1E)-[4-(dimethylamino)phenyl]methylene]sulfamide
-
pH 7.4, 25°C, isozyme hCA I
0.0000036
N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
-
pH 7.5, 20°C
0.0000749
N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
-
pH 7.5, 20°C
0.0000871
N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
-
pH 7.5, 20°C
0.000326
N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
-
pH 7.5, 20°C
0.07455
N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
-
pH 8.3, 20°C
0.001875
N-[(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]sulfamic amide
-
isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.002135
N-[(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]sulfamic amide
-
isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.00345
N-[(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]sulfamic amide
-
isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.00458
N-[(3aR,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]sulfamic amide
-
isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
0.000031
N-[4-(aminosulfonyl)phenyl]-2,2,2-trifluoroacetamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000112
N-[4-(aminosulfonyl)phenyl]-2,2,2-trifluoroacetamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00143
N-[4-(aminosulfonyl)phenyl]-2,2,2-trifluoroacetamide
pH 7.5, full-length recombinant enzyme
0.000136
N-[4-(aminosulfonyl)phenyl]-2,2-dimethylpropanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000249
N-[4-(aminosulfonyl)phenyl]-2,2-dimethylpropanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00265
N-[4-(aminosulfonyl)phenyl]-2,2-dimethylpropanamide
pH 7.5, full-length recombinant enzyme
0.000138
N-[4-(aminosulfonyl)phenyl]-2-methylpropanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000139
N-[4-(aminosulfonyl)phenyl]-2-methylpropanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.0024
N-[4-(aminosulfonyl)phenyl]-2-methylpropanamide
pH 7.5, full-length recombinant enzyme
0.000049
N-[4-(aminosulfonyl)phenyl]acetamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000135
N-[4-(aminosulfonyl)phenyl]acetamide
pH 7.5, catalytic domain of cloned isoenzyme
0.0042
N-[4-(aminosulfonyl)phenyl]acetamide
pH 7.5, full-length recombinant enzyme
0.000021
N-[4-(aminosulfonyl)phenyl]benzamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000073
N-[4-(aminosulfonyl)phenyl]benzamide
pH 7.5, catalytic domain of cloned isoenzyme
0.001345
N-[4-(aminosulfonyl)phenyl]benzamide
pH 7.5, full-length recombinant enzyme
0.000083
N-[4-(aminosulfonyl)phenyl]butanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000085
N-[4-(aminosulfonyl)phenyl]butanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00235
N-[4-(aminosulfonyl)phenyl]butanamide
pH 7.5, full-length recombinant enzyme
0.000079
N-[4-(aminosulfonyl)phenyl]pentanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000147
N-[4-(aminosulfonyl)phenyl]pentanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.0023
N-[4-(aminosulfonyl)phenyl]pentanamide
pH 7.5, full-length recombinant enzyme
0.000056
N-[4-(aminosulfonyl)phenyl]propanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.000106
N-[4-(aminosulfonyl)phenyl]propanamide
pH 7.5, catalytic domain of cloned isoenzyme
0.0037
N-[4-(aminosulfonyl)phenyl]propanamide
pH 7.5, full-length recombinant enzyme
0.0000021
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA VII
0.00001
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA VI
0.000014
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA II
0.000019
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme mCA XIII
0.000027
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA IX
0.000034
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA XII
0.000043
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA XIV
0.00005
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA I
0.000062
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA VB
0.000065
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA VA
0.00014
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme gammaCA
0.000176
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hpbetaCA
0.000225
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hpalphaCA
0.0062
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA IV
0.1
N-[5-(aminosulfonyl)-3-methyl-1,3,4-thiadiazol-2(3H)-ylidene]acetamide
isoenzyme hCA III
0.000016
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-alanine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000058
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-alanine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
0.000004
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-asparagine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000029
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-asparagine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
0.000011
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-glutamine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000053
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-glutamine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
0.000005
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-isoleucine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000025
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-isoleucine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
0.000007
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-leucine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000023
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-leucine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
0.000005
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-methionine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000031
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-methionine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
0.000008
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-phenylalanine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000042
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-phenylalanine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
0.000048
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-proline
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000197
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-proline
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
0.00002
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-tryptophan
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000064
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-tryptophan
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
0.000005
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-valine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase II
0.000031
N-[[[4-(aminosulfonyl)phenyl]amino]thioxomethyl]-L-valine
-
NovaSyn TGA-resin bound, pH 7.5, carbonic anhydrase I
4.68
N3-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
4.9
N3-
20°C, pH not specified in the publication, Co2+-substituted enzyme
5.8
N3-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
6.5
NH(SO3)22-
pH 8.3, 20°C, inhibition of CO2 hydration activity
7.9
NH(SO3)22-
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.09
nitrate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
0.46
nitrate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
36.5
nitrate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
6.8
nitrite
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
7.3
nitrite
Co(II)-substituted enzyme, pH and temperature not specified in the publication
3.15
NO2-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
6.7
NO2-
pH 8.3, 20°C, inhibition of CO2 hydration activity
6.8
NO2-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
7.3
NO2-
20°C, pH not specified in the publication, Co2+-substituted enzyme
0.09
NO3-
20°C, pH not specified in the publication, Co2+-substituted enzyme
0.99
NO3-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
5.6
NO3-
pH 8.3, 20°C, inhibition of CO2 hydration activity
21.7
NO3-
pH 8.3, 22°C, inhibition of CO2 hydration activity
36.5
NO3-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
0.000308
N~1~-(3-chloro-1H-indol-7-yl)benzene-1,4-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA34
0.000723
N~1~-(3-chloro-1H-indol-7-yl)benzene-1,4-disulfonamide
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.0007325
Orotic acid
pH 7.4, temperature not specified in the publication
1.682
Orotic acid
pH 7.4, temperature not specified in the publication
7.3
P2O74-
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.038
Ph-AsO3H2
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.0672
Ph-AsO3H2
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
0.087
Ph-AsO3H2
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.026
Ph-B(OH)2
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.088
Ph-B(OH)2
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.0055
phenol
pH 7.4, temperature not specified in the publication
0.0102
phenol
pH 7.4, temperature not specified in the publication
0.87
phenyl arsonic acid
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
30.84
phenyl arsonic acid
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.81
phenyl boronic acid
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
30.85
phenyl boronic acid
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.000086
phenylacetonitrile
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.00461
phenylacetonitrile
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.0086
phenylacetonitrile
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.674
phenylacetonitrile
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.33
phenylarsonic acid
-
20°C, pH not specified in the publication
0.4
phenylarsonic acid
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.2
phenylboronic acid
-
20°C, pH not specified in the publication
38.2
phenylboronic acid
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
7.8
ReO4-
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.0077
resorcinol
pH 7.4, temperature not specified in the publication
7.9
RuO4-
pH 8.3, 22°C, inhibition of CO2 hydration activity
8.7
RuO4-
pH 8.3, 20°C, inhibition of CO2 hydration activity
4.5
S2O82-
pH 8.3, 22°C, inhibition of CO2 hydration activity
9.1
S2O82-
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.0000403
saccharin
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.00715
saccharin
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.00796
saccharin
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.51
SCN-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
6.1
SCN-
20°C, pH not specified in the publication, Co2+-substituted enzyme
7
SCN-
20°C, pH not specified in the publication, Zn2+-substituted enzyme
9.3
SCN-
pH 8.3, 20°C, inhibition of CO2 hydration activity
7.8
SeCN-
pH 8.3, 20°C, inhibition of CO2 hydration activity
6.1
SeO42-
pH 8.3, 20°C, inhibition of CO2 hydration activity
8.3
SeO42-
pH 8.3, 22°C, inhibition of CO2 hydration activity
1.8
SnO32-
pH 8.3, 22°C, inhibition of CO2 hydration activity
6.7
SnO32-
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.33
SO42-
-
isozyme STPCA-2, pH not specified in the publication, temperature not specified in the publication
9.4
SO42-
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.33
sulfamate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.000096
sulfamic acid
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00336
sulfamic acid
20°C, pH not specified in the publication, Co2+-containing enzyme
8.22
sulfamic acid
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
44
sulfamic acid
-
20°C, pH not specified in the publication
103
sulfamic acid
-
20°C, pH not specified in the publication
0.00596
sulfamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0087
sulfamide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.069
sulfamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.99
sulfamide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
44
sulfamide
-
20°C, pH not specified in the publication
103
sulfamide
-
20°C, pH not specified in the publication
0.000037
sulfanilamide
pH 7.5, catalytic domain of cloned isoenzyme
0.00025
sulfanilamide
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.000294
sulfanilamide
pH 7.5, catalytic domain of cloned isoenzyme
0.0025
sulfanilamide
at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00393
sulfanilamide
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0054
sulfanilamide
pH 7.5, full-length recombinant enzyme
0.025
sulfanilamide
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.0578
sulfanilamide
-
20°C, pH not specified in the publication
0.58
sulfate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.00043
sulpiride
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0023
sulpiride
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00792
sulpiride
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.000006
sulthiame
isoenzyme hCA VII
0.000007
sulthiame
isoenzyme hCA II
0.000043
sulthiame
isoenzyme hCA IX
0.0000452
sulthiame
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.000081
sulthiame
isoenzyme hCA VA
0.000091
sulthiame
isoenzyme hCA VB
0.000095
sulthiame
isoenzyme hCA IV
0.000134
sulthiame
isoenzyme hCA VI
0.000374
sulthiame
isoenzyme hCA I
0.00516
sulthiame
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00525
sulthiame
isoenzyme hCA XIV
0.00672
sulthiame
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.63
sulthiame
isoenzyme hCA III
5.1
TeO42-
pH 8.3, 22°C, inhibition of CO2 hydration activity
8.5
TeO42-
pH 8.3, 20°C, inhibition of CO2 hydration activity
0.0066
tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate
pH 7.5, 22°C
0.0859
tert-butyl (2-((4-(6-methylbenzo[d]thiazol-2-yl)phenyl)amino)-2-oxoethyl)carbamate
pH 7.5, 22°C
0.0084
tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate
pH 7.5, 22°C
0.0782
tert-butyl (2-((6-(methylsulfonyl)benzo[d]thiazol-2-yl)amino)-2-oxoethyl)carbamate
pH 7.5, 22°C
0.0008
tert-butyl 3-[[(aminosulfonyl)amino]sulfonyl]phenylcarbamate
-
pH 7.4, 25°C, isozyme hCA I
0.001
tert-butyl 3-[[(aminosulfonyl)amino]sulfonyl]phenylcarbamate
-
pH 7.4, 25°C, isozyme hCA II
0.0016
tert-butyl 3-[[(aminosulfonyl)amino]sulfonyl]phenylcarbamate
-
pH 7.4, 25°C, isozyme bCA IV
0.0009
tert-butyl 4-[[(aminosulfonyl)amino]sulfonyl]phenylcarbamate
-
pH 7.4, 25°C, isozyme hCA I
0.0012
tert-butyl 4-[[(aminosulfonyl)amino]sulfonyl]phenylcarbamate
-
pH 7.4, 25°C, isozyme hCA II
0.002
tert-butyl 4-[[(aminosulfonyl)amino]sulfonyl]phenylcarbamate
-
pH 7.4, 25°C, isozyme bCA IV
0.0007
tert-butyl 5-[[(aminosulfonyl)amino]sulfonyl]-2-hydroperoxyphenylcarbamate
-
pH 7.4, 25°C, isozyme hCA I
0.0008
tert-butyl 5-[[(aminosulfonyl)amino]sulfonyl]-2-hydroperoxyphenylcarbamate
-
pH 7.4, 25°C, isozyme hCA II
0.0024
tert-butyl 5-[[(aminosulfonyl)amino]sulfonyl]-2-hydroperoxyphenylcarbamate
-
pH 7.4, 25°C, isozyme bCA IV
6.1
thiocyanate
Co(II)-substituted enzyme, pH and temperature not specified in the publication
7
thiocyanate
Zn(II)-substituted enzyme, pH and temperature not specified in the publication
55.6
thiocyanate
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-
0.94
Thiocyanide
-
at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4
0.0000009
topiramate
isoenzyme hCA VII
0.00001
topiramate
isoenzyme hCA II
0.00001
topiramate
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.0000291
topiramate
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.00003
topiramate
isoenzyme hCA VB
0.000038
topiramate
isoenzyme hCA XII
0.000045
topiramate
isoenzyme hCA VI
0.000058
topiramate
isoenzyme hCA IX
0.000058
topiramate
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000063
topiramate
isoenzyme hCA VA
0.00012
topiramate
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00025
topiramate
isoenzyme hCA I
0.00025
topiramate
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000612
topiramate
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.00102
topiramate
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00146
topiramate
isoenzyme hCA XIV
0.00146
topiramate
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00302
topiramate
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.0049
topiramate
isoenzyme hCA IV
0.0235
topiramate
-
20°C, pH not specified in the publication
0.000482
umbelliferone
-
inhibition of isozyme hCA II, pH not specified in the publication, temperature not specified in the publication
0.000754
umbelliferone
-
inhibition of isozyme hCA I, pH not specified in the publication, temperature not specified in the publication
0.0584
umbelliferone
-
inhibition of isozyme hCA XII, pH not specified in the publication, temperature not specified in the publication
0.1
umbelliferone
-
inhibition of isozyme hCA IX, pH not specified in the publication, temperature not specified in the publication
5.8
V2O74-
pH 8.3, 22°C, inhibition of CO2 hydration activity
0.000013
valdecoxib
-
isozyme CA XII, pH not specified in the publication, temperature not specified in the publication
0.000027
valdecoxib
-
isozyme CA IX, pH not specified in the publication, temperature not specified in the publication
0.0000287
valdecoxib
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.000043
valdecoxib
-
isozyme CA II, pH not specified in the publication, temperature not specified in the publication
0.00013
valdecoxib
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.00024
valdecoxib
20°C, pH not specified in the publication, Co2+-containing enzyme
0.00781
valdecoxib
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.01297
valdecoxib
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
0.054
valdecoxib
-
isozyme CA I, pH not specified in the publication, temperature not specified in the publication
0.061
valdecoxib
-
20°C, pH not specified in the publication
0.0000051
zonisamide
isoenzyme hCA IX catalytic domain
0.0000051
zonisamide
isoform CA IX, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.00002
zonisamide
isoenzyme hCA VA catalytic domain
0.000035
zonisamide
isoenzyme hCA II
0.000035
zonisamide
isoform CA II, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000056
zonisamide
isoenzyme hCA I
0.000056
zonisamide
isoform CA I, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.000089
zonisamide
isoenzyme hCA VI catalytic domain
0.000117
zonisamide
isoenzyme hCA VII catalytic domain
0.000208
zonisamide
-
at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl
0.000259
zonisamide
-
in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.00525
zonisamide
isoenzyme hCA XIV catalytic domain catalytic domain
0.00525
zonisamide
isoform CA XIV, in 10-20 mM HEPES (pH 7.5) or Tris (pH 8.3) as buffers and 20 mM Na2SO4 or 20 mM NaClO4, at 22°C
0.006033
zonisamide
isoenzyme hCA VB catalytic domain
0.00859
zonisamide
isoenzyme hCA IV catalytic domain
0.011
zonisamide
isoenzyme hCA XII catalytic domain
0.02868
zonisamide
-
at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl
2.2
zonisamide
isoenzyme hCA III
0.000295
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-2H,3aH,7H-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA31
0.0148
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-2H,3aH,7H-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCAdom
0.00001
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
wild-type, pH 7.5, 20°C
0.000038
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
pH 7.5, 20°C
0.0000855
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
pH 7.5, 20°C
0.001
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
pH 7.5, 20°C
0.00146
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
pH 8.3, 20°C
0.1
[(3aS,5aR,8aR,8bS)-2,2,7,7-tetramethyltetrahydro-3aH-bis[1,3]dioxolo[4,5-b:4',5'-d]pyran-3a-yl]methyl sulfamate
-
pH 7.5, 20°C
0.0022
[(7,7-dimethylbicyclo[2.2.1]hept-1-yl)methyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0033
[(7,7-dimethylbicyclo[2.2.1]hept-1-yl)methyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.006
[(7,7-dimethylbicyclo[2.2.1]hept-1-yl)methyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00006
[3-(trifluoromethyl)phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0002
[3-(trifluoromethyl)phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0015
[3-(trifluoromethyl)phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00003
[3-[(tert-butoxycarbonyl)amino]-4-hydroperoxyphenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0001
[3-[(tert-butoxycarbonyl)amino]-4-hydroperoxyphenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0012
[3-[(tert-butoxycarbonyl)amino]-4-hydroperoxyphenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.0008
[3-[(tert-butoxycarbonyl)amino]phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.001
[3-[(tert-butoxycarbonyl)amino]phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.01
[3-[(tert-butoxycarbonyl)amino]phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00007
[4-(acetylamino)phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0002
[4-(acetylamino)phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0015
[4-(acetylamino)phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00005
[4-[(tert-butoxycarbonyl)amino]phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0001
[4-[(tert-butoxycarbonyl)amino]phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0012
[4-[(tert-butoxycarbonyl)amino]phenyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00022
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
20°C, pH not specified in the publication, Co2+-containing enzyme
0.0022
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
20°C, pH not specified in the publication, Zn2+-containing enzyme
0.127
[4-[amino(dihydroxy)-lambda4-sulfanyl]phenyl]hydrazine
-
20°C, pH not specified in the publication
0.002
[5-(dimethylamino)-1-naphthyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.0041
[5-(dimethylamino)-1-naphthyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.008
[5-(dimethylamino)-1-naphthyl]sulfonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.000008
[[(2-methylphenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.00003
[[(2-methylphenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0003
[[(2-methylphenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00005
[[(2-methylphenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme hCA I
0.0007
[[(2-methylphenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme hCA II
0.0009
[[(2-methylphenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme bCA IV
0.000004
[[(4-chlorophenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.00002
[[(4-chlorophenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0004
[[(4-chlorophenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00005
[[(4-chlorophenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme hCA I
0.0008
[[(4-chlorophenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme hCA II
0.0011
[[(4-chlorophenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme bCA IV
0.000006
[[(4-fluorophenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.00002
[[(4-fluorophenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0003
[[(4-fluorophenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00008
[[(4-fluorophenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme hCA I
0.0009
[[(4-fluorophenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme hCA II
0.0012
[[(4-fluorophenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme bCA IV
0.00001
[[(4-methylphenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA I
0.00003
[[(4-methylphenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme hCA II
0.0006
[[(4-methylphenyl)sulfonyl]amino]carbonylsulfamic acid
-
pH 7.4, 25°C, isozyme bCA IV
0.00006
[[(4-methylphenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme hCA I
0.0011
[[(4-methylphenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme hCA II
0.0014
[[(4-methylphenyl)sulfonyl]amino]carbonylsulfamic amide
-
pH 7.4, 25°C, isozyme bCA IV
additional information
additional information
-
Ki values for natural phenols with isozymes hCA I and hCA II in the esterase activity assay, overview
-
additional information
additional information
-
Ki values of esterase activity with 4-nitrophenylacetate as substrate
-
additional information
additional information
inhibition assay using the CO2 hydration activity measurement
-
additional information
additional information
inhibition assay using the CO2 hydration activity measurement
-
additional information
additional information
inhibition assay using the CO2 hydration activity measurement
-
additional information
additional information
inhibition assay using the CO2 hydration activity measurement
-
additional information
additional information
-
inhibition assay using the CO2 hydration activity measurement
-
additional information
additional information
-
inhibition kinetics of CA isozymes, overview
-
additional information
additional information
inhibition kinetics, dissociation constants of compounds 2,3,5,6-tetrafluoro-4-(2-phenylethanesulfonyl)benzene-1-sulfonamide, 3-[[(1S)-2,3-dihydro-1H-inden-1-yl]amino]-2,5,6-trifluoro-4-(2-phenylethanesulfonyl)benzene-1-sulfonamide, 3-(benzylamino)-2,5,6-trifluoro-4-(2-hydroxyethanesulfonyl)benzene-1-sulfonamide, 3-[[(1S)-2,3-dihydro-1H-inden-1-yl]amino]-2,5,6-trifluoro-4-(2-hydroxyethanesulfonyl)benzene-1-sulfonamide and 2,3,6-trifluoro-4-(2-hydroxyethanesulfonyl)-5-[[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl]amino]benzene-1-sulfonamide binding to human recombinant CA XIV at 37°C, sodium phosphate buffer, pH 7.0
-
additional information
additional information
-
inhibition kinetics, dissociation constants of compounds 2,3,5,6-tetrafluoro-4-(2-phenylethanesulfonyl)benzene-1-sulfonamide, 3-[[(1S)-2,3-dihydro-1H-inden-1-yl]amino]-2,5,6-trifluoro-4-(2-phenylethanesulfonyl)benzene-1-sulfonamide, 3-(benzylamino)-2,5,6-trifluoro-4-(2-hydroxyethanesulfonyl)benzene-1-sulfonamide, 3-[[(1S)-2,3-dihydro-1H-inden-1-yl]amino]-2,5,6-trifluoro-4-(2-hydroxyethanesulfonyl)benzene-1-sulfonamide and 2,3,6-trifluoro-4-(2-hydroxyethanesulfonyl)-5-[[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl]amino]benzene-1-sulfonamide binding to human recombinant CA XIV at 37°C, sodium phosphate buffer, pH 7.0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2083
(1R,2S,3S,4S)-4,6-diamino-2-([3-O-[(1S,2S,3S,4S,5S)-2-amino-5-(aminomethyl)-3,4-dihydroxycyclohexyl]-alpha-L-arabinofuranosyl]oxy)-3-hydroxycyclohexyl 2,6-diamino-2,6-dideoxy-beta-L-glucopyranoside
Ovis aries
-
pH 7.4, 25°C, versus 4-nitrophenylacetate as substrate
0.2135
(2S,5R,6R)-3,3-dimethyl-7-oxo-6-(2-phenylacetamido)-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
Ovis aries
-
pH 7.4, 25°C, versus 4-nitrophenylacetate as substrate
-
0.07
(3-chlorophenyl)(2-thioxo-1H-benzo[d]imidazol-1-yl)methanone
Gallus gallus
-
pH 7.4, 37°C
0.00533
(7S)-7-[[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino]-3-[[(furan-2-carbonyl)sulfanyl]methyl]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
Ovis aries
-
pH 7.4, 25°C, versus 4-nitrophenylacetate as substrate
0.029
1-(2-thioxo-1H-benzo[d]imidazol-1-yl)-3-phenylpropan-1-one
Gallus gallus
-
pH 7.4, 37°C
0.012
1-(3-acetyl-1,2-dihydro-2-thioxobenzo[d]imidazol-1-yl)hexan-1-one
Gallus gallus
-
pH 7.4, 37°C
0.019
1-(3-ethyl-1,2-dihydro-2-thioxobenzo[d]imidazole-1-yl)ethanone
Gallus gallus
-
pH 7.4, 37°C
0.05
2,3,4,5,6-pentafluoro-N-(2-sulfamoylphenyl)benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
2,3,4,5,6-pentafluoro-N-(5-sulfamoyl-1,3,4-thiadiazol-2-yl)benzamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
2,3,4,5,6-pentafluoro-N-[(2E)-3-methyl-5-sulfamoyl-1,3,4-thiadiazol-2(3H)-ylidene]benzamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.24
2,4-Dichlorophenol
Acipenser gueldenstaedtii
-
pH 7.4, 30°C, inhibition of CO2 hydration activity
0.05
2-(7-methoxy-2-oxo-2H-chromen-4-yl)-N-(2-sulfamoylphenyl)acetamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
2-(7-methoxy-2-oxo-2H-chromen-4-yl)-N-(3-sulfamoylphenyl)acetamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
2-(7-methoxy-2-oxo-2H-chromen-4-yl)-N-(4-sulfamoylphenyl)acetamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
2-oxo-N-(2-sulfamoylphenyl)-2H-chromene-3-carboxamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
2-oxo-N-(3-sulfamoylphenyl)-2H-chromene-3-carboxamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
2-oxo-N-(4-sulfamoylbenzyl)-2H-chromene-3-carboxamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
2-oxo-N-(4-sulfamoylphenyl)-2H-chromene-3-carboxamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
2-oxo-N-[2-(4-sulfamoylphenyl)ethyl]-2H-chromene-3-carboxamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.0000151
2-[(aminooxy)sulfinyl]-5-(2-chlorophenyl)-1,3,4-thiadiazole
Saccharomyces cerevisiae
-
-
0.05
2-[(diphenylcarbamoyl)amino]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.02
3-cyclohexyl-1-(2-thioxobenzo[d]oxazol-3(2H)-yl)propan-1-one
Gallus gallus
-
pH 7.4, 37°C
0.05
4-(3-[[(1E)-(1-methyl-1H-imidazol-2-yl)methylidene]amino]propyl)benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
4-([(1E)-[4-(dimethylamino)phenyl]methylidene]amino)benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.003886
4-([[(1Z)-(2-chlorophenyl)methylidene]amino]methyl)benzenesulfonamide
Plasmodium falciparum
-
-
0.05
4-([[(diethyl-l5-azanylidyne)methyl]disulfanyl]amino)benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.000154
4-amino-N-(2-[4-[(aminooxy)sulfinyl]phenyl]ethyl)benzenesulfonamide
Saccharomyces cerevisiae
-
-
0.000166
4-amino-N-[4-[(aminooxy)sulfinyl]benzyl]benzenesulfonamide
Saccharomyces cerevisiae
-
-
0.000124
4-amino-N-[5-[(aminooxy)sulfinyl]-1,3,4-thiadiazol-2-yl]benzenesulfonamide
Saccharomyces cerevisiae
-
-
0.05
4-[([(1Z)-[4-(dimethylamino)phenyl]methylidene]amino)methyl]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
4-[([[(diethyl-l5-azanylidyne)methyl]disulfanyl]amino)methyl]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
4-[2-[(2-oxo-2H-chromen-3-yl)carbonyl]hydrazino]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
4-[2-[(7-methoxy-2-oxo-2H-chromen-4-yl)acetyl]hydrazino]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
4-[3-([(1E)-[4-(dimethylamino)phenyl]methylidene]amino)propyl]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
4-[[(1Z)-(1-bromonaphthalen-2-yl)methylidene]amino]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
4-[[(3,4-dichlorophenyl)carbamoyl]amino]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
4-[[(diphenylcarbamoyl)amino]methyl]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.00036
5-[(aminooxy)sulfinyl]-3-methyl-1,3,4-thiadiazol-2(3H)-imine
Saccharomyces cerevisiae
-
-
0.05
5-[[(pentafluorophenyl)sulfonyl]amino]-1,3,4-thiadiazole-2-sulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
5-[[(phenylcarbamoyl)carbamothioyl]amino]-1,3,4-thiadiazole-2-sulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.0165
Atrazine
Apis mellifera
-
measured with hydration of CO2 activity assay, pH and temperature not specified in the publication
0.0087
carbofuran
Apis mellifera
-
measured with hydration of CO2 activity assay, pH and temperature not specified in the publication
0.021
methyl-3-(3-phenylpropanoyl)-2,3-dihydro-2-thioxobenzo[d]oxazole-5-carboxylate
Gallus gallus
-
pH 7.4, 37°C
0.00267
N'',N'''-Bis[(E)-(2,4-dichlorophenyl)methylidene]carbonic dihydrazide
Homo sapiens
pH 7.4, 25°C
0.00146
N'',N'''-bis[(E)-(2,6-dichlorophenyl)methylidene]carbonic dihydrazide
Homo sapiens
pH 7.4, 25°C
0.00396
N'',N'''-bis[(E)-(2-bromophenyl)methylidene]carbonic dihydrazide
Homo sapiens
pH 7.4, 25°C
0.00137
N'',N'''-bis[(E)-(2-chloro-5-nitrophenyl)methylidene]carbonic dihydrazide
Homo sapiens
pH 7.4, 25°C
0.00233
N'',N'''-bis[(E)-(2-chlorophenyl)methylidene]carbonic dihydrazide
Homo sapiens
pH 7.4, 25°C
0.00185
N'',N'''-bis[(E)-(2-nitrophenyl)methylidene]carbonic dihydrazide
Homo sapiens
pH 7.4, 25°C
0.00232
N'',N'''-bis[(E)-(4-bromophenyl)methylidene]carbonic dihydrazide
Homo sapiens
pH 7.4, 25°C
0.00133
N'',N'''-bis[(E)-(4-nitrophenyl)methylidene]carbonic dihydrazide
Homo sapiens
pH 7.4, 25°C
0.05
N-[(4-[[(4-sulfamoylphenyl)carbamothioyl]amino]phenyl)sulfonyl]acetamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
N-[2,4-disulfamoyl-5-(trifluoromethyl)phenyl]-2-(7-methoxy-2-oxo-2H-chromen-4-yl)acetamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
N-[2,4-disulfamoyl-5-(trifluoromethyl)phenyl]-2-oxo-2H-chromene-3-carboxamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
N-[4-[(aminooxy)sulfinyl]phenyl]-4-[(diphenylcarbamoyl)amino]benzenesulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.05
N-[5-[(aminooxy)sulfinyl]-1,3,4-thiadiazol-2-yl]-1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonamide
Plasmodium falciparum
-
IC50 above 0.05 mM
0.102
parathion
Acipenser gueldenstaedtii
-
pH 7.4, 30°C, inhibition of CO2 hydration activity
0.016
propineb
Acipenser gueldenstaedtii
-
pH 7.4, 30°C, inhibition of CO2 hydration activity
0.0321
propoxur
Apis mellifera
-
measured with hydration of CO2 activity assay, pH and temperature not specified in the publication
0.0273
simazine
Apis mellifera
-
measured with hydration of CO2 activity assay, pH and temperature not specified in the publication
0.004
sulphanilamide
Acipenser gueldenstaedtii
-
pH 7.4, 30°C, inhibition of CO2 hydration activity
0.003
tebuconazole
Apis mellifera
-
measured with hydration of CO2 activity assay, pH and temperature not specified in the publication
0.0533
1-(4-methoxyphenyl)-2-methyl-3-nitro-1-H-indol-6-ol
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.693
1-(4-methoxyphenyl)-2-methyl-3-nitro-1-H-indol-6-ol
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.0059
4-(2-phenylacetamido)-3-bromobenzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0071
4-(2-phenylacetamido)-3-bromobenzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.263
4-(2-phenylacetamido)-3-bromobenzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.395
4-(2-phenylacetamido)-3-bromobenzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0081
4-(2-phenylacetamido)-3-chlorobenzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0082
4-(2-phenylacetamido)-3-chlorobenzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.058
4-(2-phenylacetamido)-3-chlorobenzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.061
4-(2-phenylacetamido)-3-chlorobenzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0081
4-(2-phenylacetamido)-3-fluorobenzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0083
4-(2-phenylacetamido)-3-fluorobenzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.061
4-(2-phenylacetamido)-3-fluorobenzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.067
4-(2-phenylacetamido)-3-fluorobenzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0067
4-(2-phenylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0079
4-(2-phenylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.107
4-(2-phenylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.108
4-(2-phenylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0081
4-(2-phenylacetamidoethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0082
4-(2-phenylacetamidoethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.06
4-(2-phenylacetamidoethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.067
4-(2-phenylacetamidoethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0083
4-(2-phenylacetamidomethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.054
4-(2-phenylacetamidomethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.075
4-(2-phenylacetamidomethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.086
4-(2-phenylacetamidomethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0068
4-(2-pyridin-2-ylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0068
4-(2-pyridin-2-ylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.069
4-(2-pyridin-2-ylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.075
4-(2-pyridin-2-ylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0073
4-(2-pyridin-4-ylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.009
4-(2-pyridin-4-ylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.071
4-(2-pyridin-4-ylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.074
4-(2-pyridin-4-ylacetamido)benzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0076
4-(2-pyridin-4-ylacetamidoethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0093
4-(2-pyridin-4-ylacetamidoethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.073
4-(2-pyridin-4-ylacetamidoethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.097
4-(2-pyridin-4-ylacetamidoethyl)benzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.008
4-[2-(2-thienyl)acetamidoethyl]benzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0102
4-[2-(2-thienyl)acetamidoethyl]benzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.053
4-[2-(2-thienyl)acetamidoethyl]benzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.068
4-[2-(2-thienyl)acetamidoethyl]benzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0072
4-[2-(2-thienyl)acetamidomethyl]benzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0091
4-[2-(2-thienyl)acetamidomethyl]benzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.052
4-[2-(2-thienyl)acetamidomethyl]benzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.06
4-[2-(2-thienyl)acetamidomethyl]benzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0075
4-[2-(2-thienyl)acetamido]-3-bromobenzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0087
4-[2-(2-thienyl)acetamido]-3-bromobenzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.052
4-[2-(2-thienyl)acetamido]-3-bromobenzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.084
4-[2-(2-thienyl)acetamido]-3-bromobenzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0077
4-[2-(2-thienyl)acetamido]-3-chlorobenzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0086
4-[2-(2-thienyl)acetamido]-3-chlorobenzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.05
4-[2-(2-thienyl)acetamido]-3-chlorobenzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.077
4-[2-(2-thienyl)acetamido]-3-chlorobenzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0069
4-[2-(2-thienyl)acetamido]-3-fluorobenzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0079
4-[2-(2-thienyl)acetamido]-3-fluorobenzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.161
4-[2-(2-thienyl)acetamido]-3-fluorobenzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.39
4-[2-(2-thienyl)acetamido]-3-fluorobenzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.007
4-[2-(2-thienyl)acetamido]benzenesulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0072
4-[2-(2-thienyl)acetamido]benzenesulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.05
4-[2-(2-thienyl)acetamido]benzenesulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.061
4-[2-(2-thienyl)acetamido]benzenesulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0061
5-(2-phenylacetamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0084
5-(2-phenylacetamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.051
5-(2-phenylacetamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.063
5-(2-phenylacetamido)-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0074
5-[2-(2-thienyl)acetamido]-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0076
5-[2-(2-thienyl)acetamido]-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.051
5-[2-(2-thienyl)acetamido]-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.072
5-[2-(2-thienyl)acetamido]-1,3,4-thiadiazole-2-sulfonamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.0000263
acetazolamide
Homo sapiens
-
isoform carbonic anhydrase II, using 4-nitrophenyl phosphate as substrate, at pH 7.4 and 25°C
0.000028
acetazolamide
Homo sapiens
-
isoform carbonic anhydrase II, using 4-nitrophenyl acetate as substrate, at pH 7.4 and 25°C
0.0001
acetazolamide
Acipenser gueldenstaedtii
-
pH 7.4, 30°C, inhibition of CO2 hydration activity
0.00033
acetazolamide
Homo sapiens
-
isoform carbonic anhydrase I, using 4-nitrophenyl phosphate as substrate, at pH 7.4 and 25°C
0.00049
acetazolamide
Mus musculus
-
isoform carbonic anhydrase XIII, using 4-nitrophenyl acetate as substrate, at pH 7.4 and 25°C
0.00105
acetazolamide
Mus musculus
-
isoform carbonic anhydrase XIII, using 4-nitrophenyl phosphate as substrate, at pH 7.4 and 25°C
0.00121
acetazolamide
Homo sapiens
-
isoform carbonic anhydrase I, using 4-nitrophenyl acetate as substrate, at pH 7.4 and 25°C
0.0044
acetazolamide
Chlamydomonas reinhardtii
-
isozyme CAH7, in 20 mM 4-(2-hydroxyethyl)-1-piperazine propane sulfonic acid, pH 8.0, at 4°C
0.0054
acetazolamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.012
acetazolamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.041
acetazolamide
Chlamydomonas reinhardtii
-
isozyme CAH8, in 20 mM 4-(2-hydroxyethyl)-1-piperazine propane sulfonic acid, pH 8.0, at 4°C
0.063
acetazolamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.25
acetazolamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.003
azide
Chlamydomonas reinhardtii
-
isozyme CAH7, in 20 mM 4-(2-hydroxyethyl)-1-piperazine propane sulfonic acid, pH 8.0, at 4°C
1.9
azide
Chlamydomonas reinhardtii
-
isozyme CAH8, in 20 mM 4-(2-hydroxyethyl)-1-piperazine propane sulfonic acid, pH 8.0, at 4°C
0.0462
callistephin
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.3465
callistephin
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.0031
Carbaryl
Apis mellifera
-
measured with hydration of CO2 activity assay, pH and temperature not specified in the publication
0.398
Carbaryl
Acipenser gueldenstaedtii
-
pH 7.4, 30°C, inhibition of CO2 hydration activity
0.015
cyanide
Chlamydomonas reinhardtii
-
isozyme CAH8, in 20 mM 4-(2-hydroxyethyl)-1-piperazine propane sulfonic acid, pH 8.0, at 4°C
0.061
cyanide
Chlamydomonas reinhardtii
-
isozyme CAH7, in 20 mM 4-(2-hydroxyethyl)-1-piperazine propane sulfonic acid, pH 8.0, at 4°C
0.000001
ethoxyzolamide
Pisum sativum
-
carbonic anhydrase activity of photosystem 2 membranes
0.02
ethoxyzolamide
Chlamydomonas reinhardtii
-
isozyme CAH8, in 20 mM 4-(2-hydroxyethyl)-1-piperazine propane sulfonic acid, pH 8.0, at 4°C
0.044
ethoxyzolamide
Chlamydomonas reinhardtii
-
isozyme CAH7, in 20 mM 4-(2-hydroxyethyl)-1-piperazine propane sulfonic acid, pH 8.0, at 4°C
0.1155
malvin
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.231
malvin
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.00035
oenin
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.0187
oenin
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.0013
silychristin
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.0433
silychristin
Homo sapiens
versus CO2 hydration activity, pH and temperature not specified in the publication
0.097
thiocyanate
Leptonychotes weddellii
-
pH 7.5, 20°C, inhibition of CO2 hydration activity
0.01
topiramate
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.03
topiramate
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.063
topiramate
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.25
topiramate
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.02
zonisamide
Homo sapiens
carbonic anhydrase VA, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.035
zonisamide
Homo sapiens
carbonic anhydrase II, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
0.056
zonisamide
Homo sapiens
carbonic anhydrase I, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
6.033
zonisamide
Homo sapiens
carbonic anhydrase VB, in 10 mM HEPES (pH 7.4), 0.1 M Na2SO4 or NaClO4, at 25°C
additional information
additional information
Homo sapiens
-
IC50 values for natural phenols with isozymes hCA I and hCA II in the esterase activity assay, overview
-
additional information
additional information
Dicentrarchus labrax
-
IC50 values of esterase activity with 4-nitrophenylacetate as substrate, competitive inhibition type
-
additional information
additional information
Apis mellifera
-
AmCA inhibition by the pesticides is also measured (IC50 values) using an esterase assay with 4-nitrophenylacetate as substrate
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.62
-
crude extract, using 4-nitrophenyl acetate as substrate, at pH 8.3 and 37°C
1914000
forward reaction of CO2 dehydration at 4°C in a HEPES/NaOH, pH 7.5
285000
reverse reaction of bicarbonate dehydration at 4°C in a MES/KOH pH 6.3 buffer
62.32
-
in vivo activity with supply of compressed air to the cell cultures, pH 9.0, with addition of HCO3-, pH not specified in the publication, temperature not specified in the publication
737.8
-
after 456.6fold purification, using 4-nitrophenyl acetate as substrate, at pH 8.3 and 37°C
75.2
-
in vivo activity with supply of compressed air to the cell cultures, pH not specified in the publication, temperature not specified in the publication
751.7
-
purified enzyme, esterase activity with 4-nitrophenylacetate as substrate, pH 7.5, 25°C
9.96
-
in vivo activity with supply of compressed air with added 5% CO2 to the cell cultures, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
175 EU/mg protein activity in CO2 hydration reaction, purified native enzyme, pH and temperature not specified in the publication
additional information
-
the recombinant CAH7 protein has a specific activity of 3.1 Wilbur Anderson units/mg, while the recombinant CAH8 protein has an activity of 4.2 Wilbur Anderson units/mg
additional information
specific activity 393 U/mg, enzyme units are defined as Wilbur-Anderson (WA) units
additional information
-
specific activity 393 U/mg, enzyme units are defined as Wilbur-Anderson (WA) units
additional information
-
isozyme CA-II from erythrocytes is 7.8fold more active than CA-I
additional information
-
600 EU/mg protein, purified native enzyme, pH 7.5, 20°C
additional information
-
specific activity CA-I 0.67 U/mg, specific activity CA-II 1.7 U/mg
additional information
esterase activity measurements of wild-type and mutant enzymes, pH 8.5, substrate 4-nitrophenyl acetate
additional information
-
specific activity Cam 720 units/mg, apo-Cam 20 units/mg, Co-Cam 2020 units/mg, Zn-Cam 910 units/mg, one unit = (t0-t)/t where t0 is the time for the uncatalyzed reaction and t is the time for the catalyzed reaction
additional information
-
specific activity 39.0 U/mg, one unit = (t0-t)/t, where t0 is the time for the uncatalyzed reaction and t is the time of the catalyzed reaction
additional information
-
activities of purified enzyme immobilized on different matrices, overview
additional information
-
activities of purified enzyme immobilized on different matrices, overview
additional information
-
enzyme from lysate shows a specific activity of 1.77 EU/mg, the 1280fold purified enzyme shows a specific activity of 2275 EU/mg
additional information
-
11626 EU/mg, purified enzyme, pH 7.4, 25°C, p-nitrophenylacetate substrate
additional information
-
6681.57 EU/mg, purified enzyme, pH 7.4, 25°C, p-nitrophenyl acetate substrate
additional information
-
the crude supernatant displays a specific activity of 2.44 U/mg, the 4.52fold purified enzyme shows a specific activity of 11.03 U/mg, at 25°C
additional information
-
activities of purified enzyme immobilized on different matrices, overview
additional information
-
purified native enzyme, specific activity 4130.4 EU/mg of protein
additional information
Salmo trutta Labrax Coruhensis
-
the purified enzyme from kidney has a specific activity of 603.77 EU/mg
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.5 - 10
7.6
7.8 - 8.3
assay at, the pH drops during the CO2 hydration reaction to pH 6.2
7.9
8.3
8.5
9.5
7.4
esterase activity assay at with 4-nitrophenylacetate as substrate
7.5
-
optimum pH for the esterase activity with 4-nitrophenylacetate as substrate
8.3
Halalkalibacterium halodurans
assay at, initial pH value, the value drops to pH 7.3 during the reaction
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
6 - 11
6 - 7.5
-
kcat for dehydration increases over the pH range of 6.0 to 7.5
6.5 - 10.5
-
pH profile, pH-dependent changes in the absorption spectrum of Co-HICA including an increase in molar absorptivity and a red shift of a 580 nm peak with decreasing pH, correlate with the pH-dependence of kcat/Km, overview
6.5 - 8.5
-
CO2 hydration increases over a pH range from 6.5 to 8.5
additional information
additional information
change in metal coordination from tetrahedral at pH 11.0 to a coordination consistent with a mixed population of both tetrahedral and penta-coordinate at pH 8.5 to an octahedral geometry characteristic of the oxidized enzyme Co(III)-HCA II at pH 6.0
additional information
-
change in metal coordination from tetrahedral at pH 11.0 to a coordination consistent with a mixed population of both tetrahedral and penta-coordinate at pH 8.5 to an octahedral geometry characteristic of the oxidized enzyme Co(III)-HCA II at pH 6.0
additional information
-
pH profiles for the hydration of CO2 catalyzed by wild-type HCA II and mutant Y7I HCA II, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
22
25
30
35
37
40
65
95
22
esterase activity assay at room temperature with 4-nitrophenyl acetate as substrate
25
-
optimum temperature for the esterase activity with 4-nitrophenylacetate as substrate
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
activity range, esterase activity of recombinant enzyme
13 - 30
-
13°C: about 40% of maximal activity, 30°C: about 85% of maximal activity
15 - 30
-
15°C: about 35% of maximal activity, 30°C: about 80% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
isoelectric focusing of native Ice-CA shows three bands in correspondence to pI 5.5, 5.1 and 4.8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two beta class isozymes bsCA I and bsCA II, gene BR1829
UniProt
brenda
six genes, cah-1, cah-2, cah-3, cah-4, cah-5, and cah-6, possibly encoding alpha class carbonic anhydrases
-
-
brenda
two distinct kinds of isoenzymes: high activity carbonic anhydrase and low activity carbonic anhydrase
-
-
brenda
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
UniProt
brenda
no activity in Homo sapiens
carbonic anhydrase XV is not expressed in humans, non-processed pseudogene
-
-
brenda
collected from the Northwestern coast of Sicily (Mediterranean Sea)
UniProt
brenda
-
33538, 33539, 33547, 33559, 33569, 33570, 33588, 649244, 650282, 650363, 650579, 651303, 652630, 652634, 652635, 652639, 652722, 664670, 665852, 680579, 696423, 698379, 701985, 703554, 715948, 728948
-
-
brenda
two beta class isozymes bsCA I and bsCA II, gene BR1829
UniProt
brenda
cell wall-deficient Chlamydomonas reinhardtii mutant92 (cw92), referred to as wild-type
UniProt
brenda
i.e. WL-chicken, male and female chicken, isozyme CA-II
-
-
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
SwissProt
brenda
-
SwissProt
brenda
wild-type carbonic anhydrase I and active-site mutants V62N, H67N, H200T, double-mutant V62N,H67N, and triple-mutant V62H,H67N,H200T. Wild-type carbonic anhydrase II and active site mutant enzymes N62V, N67H and T200H
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isozyme CA XII is commonly expressed in diffuse astrocytomas
brenda
-
activity of carbonic anhydrase is significantly lower in patients with renal cell carcinoma than in controls
brenda
-
isoenzyme specific for mucus of colon. Human mucus CA differs from cytosolic CAI and CAII, membrane-bound CAIV, and the secreted CAVI of saliva
brenda
DDCA is expressed predominantly in the ctenidium
brenda
very low expression level of isozyme pentraxin-carbonic anhydrase
brenda
in-situ hybridization shows that the HcCA3 is expressed in both inside and outside epidermal cells
brenda
-
fast limb muscle, high activity of isoenzyme CA3, message levels of isoenzyme CA2 and CA4 are higher in extraocular muscle than in extensor digitorum longus, expression of isoenzyme CA5 is equivalent in extraocular muscle and extensor digitorum longus
brenda
-
isoenzyme CA3 is depressed, message levels of isoenzyme CA2 and CA4 are higher in extraocular muscle than in extensor digitorum longus, expression of isoenzyme CA5 is equivalent in extraocular muscle and extensor digitorum longus
brenda
CA XIII is found mainly in surface epithelial cells of the body and antrum segments. carbonic anhydrase XIII
brenda
-
membraneous lateral wall, stria vascularis, spiral ligament, spiral prominence, outer sulcus
brenda
very low expression level of isozyme pentraxin-carbonic anhydrase
brenda
isoform hCA IX is not usually expressed in healthy tissues but is found in over 30 kinds of solid tumor cancers to date
brenda
very low expression level of isozyme pentraxin-carbonic anhydrase
brenda
-
umbilical vein endothelial cell line EA-hv926
brenda
elevated levels of extracellular carbonic anhydrase-I (CA-I) in vitreous from individuals with diabetic retinopathy, suggesting that retinal hemorrhage and erythrocyte lysis contribute to the diabetic vitreous proteome
brenda
additional information
highest expression level of isozyme pentraxin-carbonic anhydrase
brenda
-
colon expresses only the longer isoform of carbonic anhydrase XII
brenda
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
brenda
-
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
-
brenda
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
brenda
-
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
-
brenda
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
brenda
-
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
-
brenda
Pl-can temporal and spatial expression profiles, analyzed throughout embryo development by comparative quantitative PCR and whole-mount in situ hybridization (WMISH), shows that Pl-can mRNA is specifically expressed in the primary mesenchyme cells of the embryo and levels increase along with the growth of the embryonic skeleton, reaching a peak at the pluteus stage
brenda
at apical membrane of some epithelial cells surrounding the tertiary water channels and to a lesser extent at the apical membrane of some epithelial apical immunofluorescence epithelial cells as compared with the control
brenda
-
carbonic anhydrase activity is sensitive to zinc and copper inputs from the environment. Carbonic anhydrase activity is increased by zinc or iron in the range of lower Zn or Fe additions, and is inhibited by zinc or iron for the higher Zn or Fe additions. Carbonic anhydrase activity is inhibited by copper at a very low Cu addition level
brenda
-
carbonic anhydrase C2, differs from the usual C1 form by having a Cys replacement for Arg at residue 180
brenda
-
contains only the high activity isoenzyme carbonic anhydrase II
brenda
-
developmental expression profile of CA-II in erythrocytes of male and female chicken, age-related changes of CA-II levels in erythrocytes, overview
brenda
-
developmental expression profile of CA-II in erythrocytes of male and female chicken, age-related changes of CA-II levels in erythrocytes, overview
-
brenda
-
-
brenda
-
carbonic anhydrase H differs from carbonic anhydrase C in having an Asp rather than Asn at a position 9 residues removed from the COOH-terminal end of the molecule
brenda
induction of anemia causes 30-60fold increase in anaemic animals
brenda
-
about 90% of the CA activity in erythrocytes is due to the high activity CA II-like isoform, 10% are due to a low activity CA XIII isozyme
brenda
-
erythrocyte isoform CA XIII. About 90% of the CA activity in erythrocytes is due to a high activity CA II-like isoform, 10% are due to the low activity CA XIII isozyme
brenda
-
contains 2 major forms of enzyme: high-activity type and low-activity type
brenda
low transcript level, carbonic anhydrase 1
brenda
expression of the cytoplasmic isoform in the posterior gill (CasCAc) undergoes a significantly greater degree of up-regulation after exposure to low salinity (15·p.p.t.) as compared to high salinity. CasCAc has the largest scope of induction (100fold) reported for any transportrelated protein in the gill
brenda
the membrane associated isoform CasCAg is present in much higher levels of mRNA expression in both anterior and posterior gills in crabs acclimated to high salinity (35·p.p.t.) compared to crabs acclimated to low salinity
brenda
-
carbonic anhydrase activity is low and uniform across gills in shrimp acclimated to osmolarity of 30 ppt, but carbonic anhydrase activity increases in all gils after exposure to both low and high salinities. Anterior gills have the largest increases in carbonic anhydrase activity, and levels of increase are approximately the same for low and high salinity exposure. Induction of branchial carbonic anhydrase appears to be functionally important in both hyper- and hypo-osmotic regulations of hemolymph osmotic concentrations
brenda
-
pavement cells forming the gill epithelial surface layer, mucous cells, pillar cells bordering the vascular channels of the secondary lamellae, chloride cells, mitochondria-rich cells located in the primary epithelium, interlamellar regions, bases of the secondary lamellae
brenda
very low expression level of isozyme pentraxin-carbonic anhydrase
brenda
very low expression level of isozyme pentraxin-carbonic anhydrase
brenda
in both renal cortex and medulla the strongest expression is confined to the collecting ducts and weak expression can be found in the glomerulus, carbonic anhydrase XIII
brenda
-
kidney expresses only the longer isoform of carbonic anhydrase XII
brenda
expressed in cortical and medullary ducts, carbonic anhydrase XIII
brenda
strongest expression of CA XIV is detected in the cortex region, where it is restricted to the proximal tubules of S1 and S2 segments, carbonic anhydrase XIV
brenda
carbonic anhydrase 3. CA3 gene transcripts are the most abundant CA transcripts in the leaf tissues of all plants examined, being at least 50 times more plentiful than either CA1 or CA2 mRNAs. CA3 gene expression is at least 1000 times greater in leaves than in roots or flowers
brenda
low transcript level, carbonic anhydrase 1. Levels of CA1 mRNA are highest in leaves, albeit about 100fold lower than the levels of CA3 transcripts in these organs
brenda
-
low transcript level, carbonic anhydrase 1. Levels of CA1 mRNA are highest in leaves, albeit about 100fold lower than the levels of CA3 transcripts in these organs
-
brenda
-
carbonic anhydrase 3. CA3 gene transcripts are the most abundant CA transcripts in the leaf tissues of all plants examined, being at least 50 times more plentiful than either CA1 or CA2 mRNAs. CA3 gene expression is at least 1000 times greater in leaves than in roots or flowers
-
brenda
-
during the period of maximal growth (February-May), maximal activity of carbonic anhydrase is observed in fully expanded and illuminated leaves
brenda
very low expression level of isozyme pentraxin-carbonic anhydrase
brenda
-
Caplan-1 cell line, which is derived from a liver metastasis of pancreatic adenocarcinoma
brenda
-
contains carbonic anhydrase I, II and III. Male livers contain about 5times more carbonic anhydrase II than females
brenda
A0A2D1CFJ9
the pufferfish CA VI is highly expressed in liver tissue
brenda
expression in the posterior mantle pallial (pMP) is significantly higher than that in the anterior mantle pallial (aMP), and expression is low in the mantle center (MC). Expression in the aMP, pMP and MC is significantly higher in purple mussels compared with that in white mussels
brenda
-
the effect of zinc on the activity of CAIX in MDA-MB-231 breast cancer cells and membrane ghosts derived from these cells is examined. In neither setting any significant elevation of CAIX activity is measured
brenda
-
preferentially associated with the posterior midgut in both males and females
brenda
-
preferentially associated with the posterior midgut in both males and females
brenda
-
preferentially associated with the posterior midgut in both males and females
brenda
-
preferentially associated with the posterior midgut in both males and females
brenda
-
preferentially associated with the posterior midgut in both males and females
brenda
-
preferentially associated with the posterior midgut in both males and females
brenda
-
preferentially associated with the posterior midgut in both males and females
brenda
-
slow-fibre type and fast-fibre type. Slow-fibre type muscle contains carbonic anhydrase I, II and III. Fast-fibre type muscle contains carbonic anhydrase I and II
brenda
very low expression level of isozyme pentraxin-carbonic anhydrase
brenda
-
Caplan-1 cell line, which is derived from a liver metastasis of pancreatic adenocarcinoma
brenda
CA XIV is highly expressed on both the basal and apical surfaces of the pigmented epithelial cells of the retina, carbonic anhydrase XIV
brenda
-
functional carbonic anhydrase genes are more strongly expressed in green tissue, but strong expression is also found in roots for alphaCA2
brenda
-
functional carbonic anhydrase genes are more strongly expressed in green tissue, but strong expression is also found in roots for betaCA3 and betaCA6
brenda
carbonic anhydrase 2 is the most abundant carbonic anhydrase transcript in roots
brenda
very low transcript level, carbonic anhydrase 1
brenda
-
carbonic anhydrase 2 is the most abundant carbonic anhydrase transcript in roots
-
brenda
inner cortical cells, both genes encoding LjCAA1 and LjCAA2 code for nodule enhanced carbonic anhydrase isoforms, which are induced early during nodule development, overview
brenda
-
inner cortical cells, both genes encoding LjCAA1 and LjCAA2 code for nodule enhanced carbonic anhydrase isoforms, which are induced early during nodule development, overview
-
brenda
-
over 99% of the nodule enzyme is located outside the bacteroids
brenda
-
functional carbonic anhydrase genes are more strongly expressed in green tissue, but strong expression is also found in roots for alphaCA2
brenda
-
functional carbonic anhydrase genes are more strongly expressed in green tissue, but strong expression is also found in roots for betaCA3, betaCA6
brenda
tibial anterior musle and soleus muscle, broad expression of CAIII in mouse skeletal muscles. Postnatal downregulation and reexpression of CAIII in adult tibial anterior muscle
brenda
Mus musculus 129SEVE
-
tibial anterior musle and soleus muscle, broad expression of CAIII in mouse skeletal muscles. Postnatal downregulation and reexpression of CAIII in adult tibial anterior muscle
-
brenda
very low expression level of isozyme pentraxin-carbonic anhydrase
brenda
additional information
-
real-time RT-PCR analysis reveals the temporal expression pattern of genes cah-1, cah-2, cah-3, cah-4, cah-5, and cah-6
brenda
additional information
immunohistochemic analysis of enzyme distribution in zebrafish tissues, quantitative expression analysis of ca6 mRNA in wild-type and the ca6 morphant zebrafish at different stages of development
brenda
additional information
-
immunohistochemic analysis of enzyme distribution in zebrafish tissues, quantitative expression analysis of ca6 mRNA in wild-type and the ca6 morphant zebrafish at different stages of development
brenda
additional information
CA2 transcripts are equally abundant in all organs examined
brenda
additional information
CA2 transcripts are equally abundant in all organs examined
brenda
additional information
CA2 transcripts are equally abundant in all organs examined
brenda
additional information
-
CA2 transcripts are equally abundant in all organs examined
brenda
additional information
-
CA2 transcripts are equally abundant in all organs examined
-
brenda
additional information
-
the concentration of CA-II in the erythrocytes of WL-chicken is much higher than that in erythrocytes from Araucana-chicken
brenda
additional information
-
the concentration of CA-II in the erythrocytes of WL-chicken is much higher than that in erythrocytes from Araucana-chicken
-
brenda
additional information
-
the normal mucosa adjacent to the tumors also does not display expression of carbonic anhydrase IX
brenda
additional information
-
CAIX is overexpressed in many types of cancer, including breast cancer, but is most frequently absent in corresponding normal tissues
brenda
additional information
CA XIV is highly expressed in all parts of the central nervous system and to a lesser extent in adult liver, heart, small intestine, colon, kidney, urinary bladder and skeletal muscle
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CA XIV is highly expressed in all parts of the central nervous system and to a lesser extent in adult liver, heart, small intestine, colon, kidney, urinary bladder and skeletal muscle
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additional information
human carbonic anhydrase IX (hCA IX) is a tumour-associated enzyme overexpressed in several malignant human tumours
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human carbonic anhydrase IX (hCA IX) is a tumour-associated enzyme overexpressed in several malignant human tumours
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additional information
isozyme human CA II is ubiquitously-expressed
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the protein sequence of the enzyme contains a signal peptide composed of 19 amino acid residues (MVVATVILLLACAAVSNCV). Quantitative RT-PCR expression analysis and in-situ hybridization in mussel tissues, overview
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additional information
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the protein sequence of the enzyme contains a signal peptide composed of 19 amino acid residues (MVVATVILLLACAAVSNCV). Quantitative RT-PCR expression analysis and in-situ hybridization in mussel tissues, overview
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additional information
expression patterns of isozymes LjCAA1 and LjCAA2 by in situ hybridization, both are expressed in nodule inner cortical cells, vascular bundles and central tissue, overview
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additional information
expression patterns of isozymes LjCAA1 and LjCAA2 by in situ hybridization, both are expressed in nodule inner cortical cells, vascular bundles and central tissue, overview
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additional information
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expression patterns of isozymes LjCAA1 and LjCAA2 by in situ hybridization, both are expressed in nodule inner cortical cells, vascular bundles and central tissue, overview
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additional information
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expression patterns of isozymes LjCAA1 and LjCAA2 by in situ hybridization, both are expressed in nodule inner cortical cells, vascular bundles and central tissue, overview
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additional information
immunohistochemic analysis using monoclonal antibody against CP3, mAb CP3, detailed overview. No CAIII is detected by CP3 in mouse heart and bladder smooth muscle, or in extensor digitorum longus muscle
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immunohistochemic analysis using monoclonal antibody against CP3, mAb CP3, detailed overview. No CAIII is detected by CP3 in mouse heart and bladder smooth muscle, or in extensor digitorum longus muscle
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Mus musculus 129SEVE
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immunohistochemic analysis using monoclonal antibody against CP3, mAb CP3, detailed overview. No CAIII is detected by CP3 in mouse heart and bladder smooth muscle, or in extensor digitorum longus muscle
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additional information
unlike isoenzyme TCAb, isoenzyme TCAc lacks tissue specificity and may be expressed in the cytoplasm of all cells
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additional information
unlike isoenzyme TCAb, isoenzyme TCAc lacks tissue specificity and may be expressed in the cytoplasm of all cells
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additional information
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unlike isoenzyme TCAb, isoenzyme TCAc lacks tissue specificity and may be expressed in the cytoplasm of all cells
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additional information
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heart, liver and muscle have negligible levels of cytoplasmic carbonic anhydrase activity
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additional information
A0A2D1CFJ9
quantitative and semiquantitative RT-PCR expression analysis and in situ hybridization
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additional information
the DDCA is localized apically in certain epithelial cells near the base of the ctenidial filament and the epithelial cells surrounding the tertiary water channels. No or very poor expression in inner mantle, foot muscle, byssal muscle, heart, hepatopancreas, and kidney of Tridacna squamosa kept in darkness for 12 h, immunofluorescent tissue distribution analysis
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the DDCA is localized apically in certain epithelial cells near the base of the ctenidial filament and the epithelial cells surrounding the tertiary water channels. No or very poor expression in inner mantle, foot muscle, byssal muscle, heart, hepatopancreas, and kidney of Tridacna squamosa kept in darkness for 12 h, immunofluorescent tissue distribution analysis
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additional information
the outer mantle, which contains the highest density of tertiary tubules and exosymbiont zooxanthellae, displays high level of CA2-like expression, and CA2-like is localized to the tubule epithelial cells. Cloning of CA2 homolog (CA2-like) from the fleshy and colorful outer mantle as well as the thin and whitish inner mantle of Tridacna squamosa to determine its cellular and subcellular localization. Immunofluorescent enzyme localization study
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
alpha-type CA (CrCAH3) locates in the thylakoid lumen
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CsoSCA exists within the carboxysome shell either as a homodimer or as extended filaments
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enzyme shows activity only in carboxysomal fraction
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murine sperm possesses extracellular isozyme CA IV that is transferred to the sperm surface as the sperm pass through the epididymis, the transfer takes place in the corpus epididymidis
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murine sperm possesses extracellular isozyme CA IV that is transferred to the sperm surface as the sperm pass through the epididymis, the transfer takes place in the corpus epididymidis
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betaCA1 and betaCA5 are targeted to the chloroplast
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in vitro import assays shows CA1 is imported into isolated chloroplast of Pisum sativum
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in vitro import assays shows CA1 is imported into isolated chloroplast of Pisum sativum
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the soluble PtCA1 is targeted to the stroma by the bipartite sequence of Pre46AA (N-terminal presequence of 46 amino acids that does not exist in the mature PtCA1)
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CA1 but not CA2 is localized in the chloroplast
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CA1 but not CA2 is localized in the chloroplast
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CA9 is expressed along the cytoplasmic membrane of tumor cells
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extracellular membrane-bound
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murine sperm possesses extracellular isozyme CA IV that is transferred to the sperm surface as the sperm pass through the epididymis, the transfer takes place in the corpus epididymidis
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murine sperm possesses extracellular isozyme CA IV that is transferred to the sperm surface as the sperm pass through the epididymis, the transfer takes place in the corpus epididymidis
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the enzyme is anchored to membrane surface by a phosphatidylinositol-glycan linkage
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carbonic anhydrase IV is associated with a lipid or a glycolipid membrane fraction
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at least half of the carbonic anhydrase IV in lung and kidney is anchored to membranes by phosphatidylinositol-glycan linkages
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carbonic anhydrase IV is detected in the apical membrane of polarized cells
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membrane protein overexpressed in certain cancer tumor cells
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transmembrane glycoprotein with an active extracellular CA domain
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isoforms CA XIV, CA IX and CA XII are transmembrane proteins
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CA IX is a transmembrane protein, where the extracellular region consists of the catalytic CA domain and the proteoglycan-like (PG) domain
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extracellular membrane-bound
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glycosylphosphatidylinositol-anchored membrane protein
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membrane-bound, at apical membrane of some epithelial cells surrounding the tertiary water channels and to a lesser extent at the apical membrane of some epithelial apical immunofluorescence epithelial cells as compared with the control. Presence of two transmembrane regions in the DDCA
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association of the enzyme with light microsomal membranes is dependent on pH, being lower at neutral or alkaline pH. 2 Enzyme forms: a loosely-membrane-associated enzyme and a firmly-membrane-associated enzyme
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contain N-terminal signal peptide for translocation into mitochondria
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betaCA4 is targeted to the plasma membrane
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CAIX is the only membrane-associated carbonic anhydrase inMDA-MB-231 cells. EGF induces CAIX translocation to lipid rafts
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the enzyme is associated exclusively with the plasma membrane
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apical and basal plasma membrane of proximal tubuli
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apical and basal plasma membrane of proximal tubuli
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in extensor digitorum longus. Extraocular muscle has very low sarcolemmal or cytosolic carbonic anhydrase activity
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membrane. Activity of photosystem 1 membranes if calculated on chlorophyll basis is much higher than the activity of photosystem 2 membranes
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complexed with rubisco on the outer surface of thylakoids
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outer peripheral, inner peripheral or integral localization
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enzyme CrCAH3 is associated with photosystem II, PSII
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enzyme CrCAH3 is associated with photosystem II, PSII
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subcellular localization study, overview
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CcaA's recruitment to the carboxysome relies upon interacting with CcmM by aligning their mutual three-fold symmetry axes
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Synechocystis sp. PCC 6803 / Kazusa
CcaA's recruitment to the carboxysome relies upon interacting with CcmM by aligning their mutual three-fold symmetry axes
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the signal peptide (residue 1-22) is predicted to be extracellular, and the GPI anchor is predicted to be Ala576 located near the 3' end of the second CA domain
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the signal peptide (residue 1-22) is predicted to be extracellular, and the GPI anchor is predicted to be Ala576 located near the 3' end of the second CA domain
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
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carbonic anhydrase represents one of the most ancient proteins
evolution
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carbonic anhydrase represents one of the most ancient proteins
evolution
evolutionary tree of some bacterial beta-CAs among which the two Brucella suis isozymes bsCA I and bsCA II, phylogenetic analysis, overview
evolution
HICA is a type II member of the beta-carbonic anhydrase family
evolution
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phylogenetic analysis of beta-class carbonic anhydrases in invertebrates, overview
evolution
Salmo trutta Labrax Coruhensis
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carbonic anhydrase is a member of zinc-containing metalloenzyme family
evolution
A0A2D1CFJ9
comparisons of putative active site residues between CA II and CA VI from humans and several fishes
evolution
evolutionary relationship analysis, phylogenetic tree, the enzyme belongs to the beta class of carbonic anhydrases, subgroup of type II beta-CAs. The enzyme B13-CA has all the features of a catalytically effective beta-CA: (i) the putative Zn(II) ligands, Cys42, Asp44, His 98 and Cys101, (ii) the catalytic dyad involved in activation of the zinc-coordinated water molecule/hydroxide ion for catalysis, represented by the Asp44-Arg46 residues, which resembles in a way the activation of the water molecule in aspartic proteases
evolution
phylogenetic analysis indicates that Pl-CAN is evolutionarily closer to humans among chordates than to other species
evolution
several genetically distinct classes of carbonic anhydrase (CAs) exist, e.g. alpha-, beta-, gamma-, delta- and zeta-, and all of them are metalloenzymes. delta-CAs are closer to the alpha-CAs than to the other classes of the enzymes, phylogenetic analysis
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
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the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
evolution
the enzyme belongs to the eta-CA class. Six genetically distinct CA families are known to date, the alpha-, beta-, gamma-, delta-, zeta- and eta-CAs. The alpha-, beta-, delta- and probably eta-CAs use Zn(II) ions at the active site, the gamma-CAs are probably Fe(II) enzymes, but they are active also with bound Zn(II) or Co(II) ions, whereas the zeta-class are cambialistic enzymes, active both with Cd(II) or Zn(II) bound within the active site
evolution
the enzyme belongs to the superfamily of metalloenzymes
evolution
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evolutionary tree of some bacterial beta-CAs among which the two Brucella suis isozymes bsCA I and bsCA II, phylogenetic analysis, overview
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evolution
Persephonella marina DSM 14350 / EX-H1
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the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
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evolution
Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1
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the dimeric arrangement is a peculiar feature of all bacterial alpha-CAs so far structurally characterized
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malfunction
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isozyme CAIX expression and activity is associated with metabolic dysfunction in MDA-MB-231 cells
malfunction
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CA IV-/- mice show a 32.13% reduction in total carbonic anhydrase activity and reduced beat frequency compared to the wild-type
malfunction
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analyses of a cpb deletion mutant shows that Cpb is strictly required for growth when cultured in semi-defined medium and an atmosphere without CO2. Growth of the mutant is the same as that of the parent wild-type strain when cultured in nutrient-rich media with or without CO2 in the atmosphere, although elimination of glucose results in decreased production of acetate, propionate, and butyrate
malfunction
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at very low CO2 concentrations eCA inhibition reduces photosynthesis
malfunction
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at very low CO2 concentrations enzyme inhibition reduces photosynthesis
malfunction
enzyme complements Saccharomyces cerevisiae deletion mutant Nce103
malfunction
a CrCIA3 deletion mutant shows 50% reduction of the O2 evolution rate
malfunction
Arabidopsis thaliana mutants defective in two CA subunits show an altered photorespiratory phenotype. Mutants grown in ambient air show growth retardation compared to wild-type plants, a feature that is reversed by cultivating plants in a high-CO2 atmosphere. Under photorespiratory conditions, carbon assimilation is diminished and glycine accumulates, suggesting an imbalance with respect to photorespiration. Additionally, transcript levels of specific CA subunits are reduced in plants grown under non-photorespiratory conditions, leaves of ca2cal1 and ca2cal2 double mutants exhibited increased ROS levels. Mutants ca2cal1 and ca2cal2 show growth retardation in normal air. Mutant phenotypes, overview
malfunction
Arabidopsis thaliana mutants defective in two CA subunits show an altered photorespiratory phenotype. Mutants grown in ambient air show growth retardation compared to wild-type plants, a feature that is reversed by cultivating plants in a high-CO2 atmosphere. Under photorespiratory conditions, carbon assimilation is diminished and glycine accumulates, suggesting an imbalance with respect to photorespiration. Additionally, transcript levels of specific CA subunits are reduced in plants grown under non-photorespiratory conditions. Mutant phenotypes, overview
malfunction
loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, mitochondrial function, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress. Car3-KO increases the resistance of soleus muscle to acidosis
malfunction
swimming pattern analysis of ca6 morphant and wild-type zebrafish, mutant phenotype of ca6 knockout fish, overview
malfunction
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CA IV-/- mice show a 32.13% reduction in total carbonic anhydrase activity and reduced beat frequency compared to the wild-type
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malfunction
Mus musculus 129SEVE
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loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, mitochondrial function, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress. Car3-KO increases the resistance of soleus muscle to acidosis
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physiological function
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beta carbonic anhydrase is required for scavenging CO2 from the ambient air
physiological function
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isoform CA IX is involved in tumorigenesis through many pathways, such as pH regulation and cell adhesion control
physiological function
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CAIX is a zinc metalloenzyme that catalyzes the reversible hydration of CO2. CAIX expression is strongly induced by hypoxia and is significantly associated with tumor grade and poor survival
physiological function
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isoyzme CAII is associated with the acute mountain sickness, a common disease at high altitude
physiological function
isozyme LjCAA1 is involved in nitrogen ficxation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
physiological function
isozyme LjCAA2 is involved in nitrogen fixation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
physiological function
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role of isozyme carbonic anhydrase IV in the bicarbonate-mediated activation of sperm, overview. Sperm respond to CO2 with an increase in beat frequency, an effect that can be inhibited by ethoxyzolamide. CA IV supplies sperm with HCO3-, which is necessary for stimulation of atypical sperm adenylyl cyclase and hence early activation of spermatozoa
physiological function
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role of isozyme carbonic anhydrase IV in the bicarbonate-mediated activation of sperm, overview. Sperm respond to CO2 with an increase in beat frequency, an effect that can be inhibited by ethoxyzolamide. CA IV supplies sperm with HCO3-, which is necessary for stimulation of atypical sperm adenylyl cyclase and hence early activation of spermatozoa
physiological function
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the enzyme from chicken has an important role in eggshell formation
physiological function
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a theoretical model predicts that homogeneous cytoplasmic distribution of CAII is more favourable for cellular transport of HCO3- and CO2 than is association of CAII with the cytoplasmic surface of the plasma membrane. Physiological interference with anion exchanger AE1 could not be demonstrated
physiological function
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carbonic anhydrase which displays significant catalytic activity in intact oocytes, also reduces the SNAT3-associated membrane conductance, when glutamine, but not when asparagine is the substrate
physiological function
CA2-like can probably take part in the increased supply of inorganic carbon (Ci) from the host clam to the symbiotic zooxanthellae when the latter conduct photosynthesis to fix Ci during light exposure
physiological function
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carbonic anhydrase (CA) is a ubiquitously expressed metalloenzyme that catalyses the hydration and dehydration reactions of carbon dioxide and bicarbonate, respectively. This basic reaction has innumerable physiological and biochemical associations and consequently CA isoforms are found in virtually all living organisms
physiological function
carbonic anhydrase (CA) plays a key role in neuronal signaling, providing bicarbonate and proton ions for GABAergic and glutamatergic neuronal function. Activation of CA isoforms expressed in neurons have been shown to have implications in the prognosis of Alzheimer's disease and dementia, while inhibitors of CAs are clinically used in the treatment of epilepsy, emphasizing the importance of this family of enzymes in both disease and normal neuronal function
physiological function
Halalkalibacterium halodurans
carbonic anhydrase is a biocatalyst that catalyzes the hydration of CO2to bicarbonate and protons, and an alkalistable and moderately thermostable alpha-carbonic anhydrase
physiological function
carbonic anhydrase VA (CAVA) is a mitochondrial enzyme that catalyzes the reversible hydration of CO2 to produce HCO3- and proton. CAVA is primarily involved in several biosynthetic processes such as ureagenesis, gluconeogenesis and lipogenesis by providing bicarbonate ion
physiological function
carbonic anhydrases are key enzymes involved in the acquisition of inorganic carbon for photosynthesis in phytoplankton, as they catalyze efficiently the interconversion between carbon dioxide and bicarbonate
physiological function
Synechocystis sp. PCC 6803 / Kazusa
CcaA is a beta-carbonic anhydrase that is a component of the carboxysomes of a subset of beta-cyanobacteria. It has a characteristic C-terminal extension and is recruited to the carboxysome via interactions with CcmM, UniProt ID P72758, which is itself a gamma-CA homologue with enzymatic activity in many, but not all cyanobacteria. Enzyme CcaA forms a complex with CcmM with sub-picomolar affinity, with contributions from residues in CcmM's alphaA helix and CcaA's C-terminal tail. Enzyme Cca shows low activity compared to other CAs, the C-terminal tail appears to partly inhibit activity, possibly indicating a role in minimizing the activity of unencapsulated enzyme. The need for the HCO3- entering the carboxysome to be efficiently converted into CO2 requires that carbonic anhydrase is co-encapsulated within the carboxysome. On the other hand, the presence of CA activity in the cytosol is highly deleterious as it converts the accumulated HCO3- into its membrane-permeable CO2 counterpart outside of the protective barrier afforded by the shell. Intracellular CAs in cyanobacteria are required to possess interaction determinants that target them to the carboxysome, as well as mechanisms that minimize CA activity prior to the completion of the shell. CcmM is the second potential beta-carboxysomal CA and is universally present in beta-carboxysomes as it functions as a central nexus for organizing the carboxysome's interior. Formation of the CcaA/CcmM complex probably requires significant backbone movements in at least one of the binding partners. CcaA is among the least active beta-CAs characterized to date, with activity comparable with the gamma-CA, CcmM
physiological function
CcmM is itself a gamma-carbonic anhydrase homologue with enzymatic activity. It has a characteristic C-terminal extension and is recruited to the carboxysome via interactions with CcmM, which is itself a gamma-CA homologue with enzymatic activity in many, but not all cyanobacteria. Enzyme CcaA forms a complex with CcmM with sub-picomolar affinity, with contributions from residues in CcmM's alphaA helix and CcaA's C-terminal tail. CcaA is recruited to the beta-carboxysome by binding the N-terminal domain of CcmM. Enzyme Cca shows low activity compared to other CAs, the C-terminal tail appears to partly inhibit activity, possibly indicating a role in minimizing the activity of unencapsulated enzyme. The need for the HCO3- entering the carboxysome to be efficiently converted into CO2 requires that carbonic anhydrase is co-encapsulated within the carboxysome. On the other hand, the presence of CA activity in the cytosol is highly deleterious as it converts the accumulated HCO3- into its membrane-permeable CO2 counterpart outside of the protective barrier afforded by the shell. Intracellular CAs in cyanobacteria are required to possess interaction determinants that target them to the carboxysome, as well as mechanisms that minimize CA activity prior to the completion of the shell. CcmM is the second potential beta-carboxysomal CA and is universally present in beta-carboxysomes as it functions as a central nexus for organizing the carboxysome's interior. Formation of the CcaA/CcmM complex probably requires significant backbone movements in at least one of the binding partners. CcaA is among the least active beta-CAs characterized to date, with activity comparable with the gamma-CA, CcmM. CcmM is the second potential beta-carboxysomal CA and is universally present in beta-carboxysomes as it functions as a central nexus for organizing the carboxysome's interior. CcmM is built as two distinct regions, the C-terminal region of CcmM consists of three to five repeats of a RubisCO small subunit-like domain, separated by flexible linker regions, this region binds RubisCO. The N-terminal domain is clearly homologous to gamma-CAs, but in Synechocystis sp. PCC 6803, this domain lacks measurable CA activity
physiological function
expressing similar fast type of myofilament proteins, CAIII-positive tibial anterior muscle exhibits higher tolerance to fatigue than that of CAIII-negative fast twitch extensor digitorum longus muscle in in situ contractility studies
physiological function
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gamma-CAs are present in carboxysomes, being involved in photosynthesis
physiological function
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gamma-CAs are widely distributed in all three phylogenetic domains of life, playing important roles in the global carbon cycle
physiological function
gamma-CAs are widely distributed in all three phylogenetic domains of life, playing important roles in the global carbon cycle
physiological function
human carbonic anhydrase IX (hCA IX) is a tumour-associated enzyme. The observed conformational flexibility of the enzyme's extrcellular PG domain may have several important roles in tumour progression, facilitating interactions of hCA IX with partner proteins assisting tumour spreading and progression
physiological function
Hyriopsis cumingii isozyme HcCA3 play a role in the formation of shell and pearl sac formation. The mantle epithelial cell of acceptor mussels sharply divide and proliferate after being stimulated and wrap the stimulus to form pearl sac gradually. Pearl sac gradually secretes pearl essence layer by layer around stimulus and form pearl ultimately. HcCA3 expression in different parts of the mantle shows different trends during pearl formation, which suggests that it plays different roles in the process
physiological function
in metazoans, the alpha-CA family is largely represented and plays a pivotal role in the deposition of calcium carbonate biominerals
physiological function
in the green alga Chlamydomonas reinhardtii, a luminal carbonic anhydrase, CrCAH3 improves proton removal from phorosystem PSII, possibly by rapid reformation of HCO3- from CO2. It plays a direct role of CrCAH3 in the turnover efficiency of PSII, and a stimulating effect of CrCAH3 and CO2/HCO3- on PSII activity. Possible redox regulation of the enzyme, overview. Redox regulation in the chloroplast thylakoid lumen is a common way to regulate lumenal and photosynthetic proteins
physiological function
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polyhemoglobin-superoxide dismutase-catalase-carbonic anhydrase (poly-[Hb-SOD-CAT-CA]) contains all three major functions of red blood cells (RBCs) at an enhanced level. The crosslinked poly-[SFHb-SOD-CAT-CA] enzyme complex does not activate the complement pathway in rat plasma
physiological function
A0A2D1CFJ9
pufferfish CA VI is an extracellular secretory protein
physiological function
Halalkalibacterium halodurans
the carbonic anhydrase catalyzed hydration of CO2 is fundamental to many vital physiological functions in living organisms such as pH homeostasis, ion transport, carbon concentrating mechanism (plants and many microorganisms), and in biosynthesis of physiologically important metabolites
physiological function
the ctenidial DDCA is positioned to dehydrate HCO3- to CO2 in seawater, and to hydrate the CO2 that has permeated the apical membrane back to HCO3- in the cytoplasm. During insolation, the host clam needs to increase the uptake of inorganic carbon from the ambient seawater to benefit the symbiotic zooxanthellae. Only then can the symbionts conduct photosynthesis and share the photosynthates with the host. Enzyme DDCA might participate in the light-enhanced uptake and assimilation of exogenous inorganic carbon
physiological function
the Mytilus galloprovincialis alpha-CA is involved in pH regulation and/or in the delivery of bicarbonate helping the mussel during the formation of the shell
physiological function
the NADH-ubiquinone oxidoreductase complex (complex I, EC 1.6.5.3) is the main entrance site of electrons into the respiratory chain. In a variety of eukaryotic organisms, except animals and fungi (Opisthokonta), it contains an extra domain comprising trimers of putative gamma-carbonic anhydrases, named the CA domain, which has been proposed to be essential for assembly of complex I. The CA domain of plant complex I contributes to sustaining efficient photosynthesis under ambient (photorespiratory) conditions. The CA protein domain contains at least two different gamma-CA proteins, CA1 (At1g19580) and CA2 (At1g47260), which show conserved active-site regions, and two less well-conserved gamma-CA-like proteins, CAL1 (At5g63510) and CAL2 (At3g48680), containing non-conservative replacements of putatively important amino acids
physiological function
Halalkalibacterium halodurans TSLV1
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carbonic anhydrase is a biocatalyst that catalyzes the hydration of CO2to bicarbonate and protons, and an alkalistable and moderately thermostable alpha-carbonic anhydrase
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physiological function
Halalkalibacterium halodurans TSLV1 / MTCC 10961
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the carbonic anhydrase catalyzed hydration of CO2 is fundamental to many vital physiological functions in living organisms such as pH homeostasis, ion transport, carbon concentrating mechanism (plants and many microorganisms), and in biosynthesis of physiologically important metabolites
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physiological function
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role of isozyme carbonic anhydrase IV in the bicarbonate-mediated activation of sperm, overview. Sperm respond to CO2 with an increase in beat frequency, an effect that can be inhibited by ethoxyzolamide. CA IV supplies sperm with HCO3-, which is necessary for stimulation of atypical sperm adenylyl cyclase and hence early activation of spermatozoa
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physiological function
Mus musculus 129SEVE
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expressing similar fast type of myofilament proteins, CAIII-positive tibial anterior muscle exhibits higher tolerance to fatigue than that of CAIII-negative fast twitch extensor digitorum longus muscle in in situ contractility studies
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physiological function
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beta carbonic anhydrase is required for scavenging CO2 from the ambient air
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physiological function
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the enzyme from chicken has an important role in eggshell formation
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physiological function
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isozyme LjCAA1 is involved in nitrogen ficxation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
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physiological function
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isozyme LjCAA2 is involved in nitrogen fixation/assimilation, but may also be involved in biochemical and physiological processes not directly linked to nitrogen fixation/assimilation
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additional information
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EGF induces CAIX translocation to lipid rafts but not its phosphorylation
additional information
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evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase
additional information
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evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase
additional information
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Pseudomonas fragi, Micrococcus lylae and Micrococcus luteus 2 along with a comparative evaluation of their efficiency compared to commercial Bis taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, aparameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous CAs and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine CA
additional information
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Pseudomonas fragi, Micrococcus lylae and Micrococcus luteus 2 along with a comparative evaluation of their efficiency compared to commercial Bis taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, aparameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous CAs and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine CA
additional information
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the wide use of dithiocarbamate pesticides may be one of the factors enhancing the vulnerability of this sturgeon species to pollutants, since they act as effective carbonate dehydratase inhibitors
additional information
a disulfide bond between Cys90 and Cys258 is essential for CrCAH3 activity
additional information
-
a disulfide bond between Cys90 and Cys258 is essential for CrCAH3 activity
additional information
a key role for sodium ions in increasing halotolerant enzyme stability largely through interactions with the highly ordered first Na+ hydration shell, molecular dynamics calculations, overview
additional information
Synechocystis sp. PCC 6803 / Kazusa
CcaA is crystallized at pH 4.5 but remains in the active, type I conformation, which is typified by a salt bridge between Asp41 and Arg43 that allows the zinc ion to remain free for substrate binding. In addition, CcaA does not show the co-operative inactivation at low pH characteristic of the type II bacterial enzymes (see below), and the residues that form the non-catalytic (regulatory) bicarbonate-binding site (Arg-Trp-Tyr) are absent. CcaA is a structurally characterized bacterial beta-CA that displays type I active sites
additional information
enzyme structure, catalytic mechanism, and molecular dynamics simulations
additional information
-
enzyme structure, catalytic mechanism, and molecular dynamics simulations
additional information
homology modeling of isozyme CA VI including PTX domain (residues 317-530) using the structure of human isozyme CA IV as template, PDB ID 3FE4. Structure comparisons
additional information
-
homology modeling of isozyme CA VI including PTX domain (residues 317-530) using the structure of human isozyme CA IV as template, PDB ID 3FE4. Structure comparisons
additional information
A0A2D1CFJ9
homology modeling of puffer CA VI is performed using the crystal structure of human carbonic anhydrase XIV as a template structure
additional information
homology modeling of Synechocystis CcmM
additional information
identification of the structural features responsible for the high catalytic activity of the enzyme from Sulfurihydrogenibium azorense, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein. On the bottom of this cavity, the catalytic zinc ion is tetrahedrally coordinated by the three histidine residues (His89, His91 and His108). Enzyme SazCA active site structure and environment, important for catalytic activity, overview
additional information
-
identification of the structural features responsible for the high catalytic activity of the enzyme from Sulfurihydrogenibium azorense, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein. On the bottom of this cavity, the catalytic zinc ion is tetrahedrally coordinated by the three histidine residues (His89, His91 and His108). Enzyme SazCA active site structure and environment, important for catalytic activity, overview
additional information
isozyme modelling and molecular dynamics studies, overview
additional information
-
isozyme modelling and molecular dynamics studies, overview
additional information
residue Thr477 in PfCAdom is crucial for its catalysis
additional information
-
residue Thr477 in PfCAdom is crucial for its catalysis
additional information
Halalkalibacterium halodurans
residues H137, H139, H156, and H110 present in the active site play an important role in catalysis, the active site of recombinant BhCA is also composed of conserved Glu and Asp acid residues
additional information
structure analysis. Enzyme Cab shows significant structural differences with respect to the other enzymes of beta-class in the N-terminus, C-terminus and in the region encompassing residues 90-125. Moreover, it presents a less extended C-terminal region, being the smallest beta-CA so far characterized
additional information
structure comparisons, residues His2 and His207 in enzyme SazCA from Sulphurihydrogenibium azorense, as compared to Glu2 and Gln207 in enzyme SspCA from Sulfurihydrogenibium yellowstonense, are proposed to be responsible for the higher SazCA catalytic activity
additional information
-
structure comparisons, residues His2 and His207 in SazCA, compared Glu2 and Gln207 in enzyme SspCA from Sulfurihydrogenibium yellowstonense, are proposed to be responsible for the higher SazCA catalytic activity
additional information
the 69 amino acid residues insertion present in the active site of eta-CA PfCAdom seem to be crucial for the active site architecture
additional information
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the 69 amino acid residues insertion present in the active site of eta-CA PfCAdom seem to be crucial for the active site architecture
additional information
the CA domain of the enzyme includes 7 active site residues: His93, Gln128, His130, His132, Glu142, His155 and Thr248. Residues His130, His132, and His155 are zinc iron binding sites
additional information
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the CA domain of the enzyme includes 7 active site residues: His93, Gln128, His130, His132, Glu142, His155 and Thr248. Residues His130, His132, and His155 are zinc iron binding sites
additional information
the deduced enzyme DDCA sequence contains two distinct alpha-CA domains, each with a specific catalytic site. Each alpha-CA domain of the DDCA has its own set of catalytic and active sites. The first alpha-CA domain comprised the three histidine residues (His116, His118, His141) which coordinate the Zn2+-containing catalytic site, the hydrophobic residues (Val143, Val164, Leu224, Val233, Trp235) that form the CO2 binding pocket, and the gatekeeper residues (Glu128, Thr226). In the first alpha-CA domain, the active binding site for HCO3- and H+ constitutes five hydrophilic residues (Asn85, His87, Gln114, Thr225, and Thr226), of which His87 acts as a proton shuttle for CO2 hydration. Similarly, the Zn2+-containing catalytic site (His391, His393, His416), the hydrophobic residues that form the CO2 binding pocket (Val418, Val439, Leu504, Val513, Trp515), and the gatekeeper residues (Glu403, Thr506) are conserved in the second alpha-CA domain. Unlike the first alpha-CA domain, six hydrophilic residues (Asn361, His363, Gln366, Gln389, Thr505, and Thr506) are found in the second alpha-CA domain, and His363 serves as a proton shuttle for CO2 hydration
additional information
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the deduced enzyme DDCA sequence contains two distinct alpha-CA domains, each with a specific catalytic site. Each alpha-CA domain of the DDCA has its own set of catalytic and active sites. The first alpha-CA domain comprised the three histidine residues (His116, His118, His141) which coordinate the Zn2+-containing catalytic site, the hydrophobic residues (Val143, Val164, Leu224, Val233, Trp235) that form the CO2 binding pocket, and the gatekeeper residues (Glu128, Thr226). In the first alpha-CA domain, the active binding site for HCO3- and H+ constitutes five hydrophilic residues (Asn85, His87, Gln114, Thr225, and Thr226), of which His87 acts as a proton shuttle for CO2 hydration. Similarly, the Zn2+-containing catalytic site (His391, His393, His416), the hydrophobic residues that form the CO2 binding pocket (Val418, Val439, Leu504, Val513, Trp515), and the gatekeeper residues (Glu403, Thr506) are conserved in the second alpha-CA domain. Unlike the first alpha-CA domain, six hydrophilic residues (Asn361, His363, Gln366, Gln389, Thr505, and Thr506) are found in the second alpha-CA domain, and His363 serves as a proton shuttle for CO2 hydration
additional information
the full nucleotide sequence encoding for the native MgaCA shows an open reading frame of 255 amino acid residues containing the conserved three histidines, His94, His96, and His119 (hCA I numbering system), which coordinate the Zn(II) ion crucial for catalysis, and the two gate-keeper residues, the Glu106 and Thr199. The mussel enzyme has a residue of lysine as substituent of the proton shuttle residue His64, explaining the relatively low catalytic activity of the native MgaCA, with the following kinetic parameters for the CO2 hydration reaction
additional information
-
the full nucleotide sequence encoding for the native MgaCA shows an open reading frame of 255 amino acid residues containing the conserved three histidines, His94, His96, and His119 (hCA I numbering system), which coordinate the Zn(II) ion crucial for catalysis, and the two gate-keeper residues, the Glu106 and Thr199. The mussel enzyme has a residue of lysine as substituent of the proton shuttle residue His64, explaining the relatively low catalytic activity of the native MgaCA, with the following kinetic parameters for the CO2 hydration reaction
additional information
the Mytilus galloprovincialis alpha-CA sequence contains the three His residues (His94, His96, and His119) acting as zinc ligands and the gate-keeper residues present in all alpha-CAs (Glu106 and Thr199), but has a Lys in position 64 and not a His as proton shuttling residue
additional information
-
the Mytilus galloprovincialis alpha-CA sequence contains the three His residues (His94, His96, and His119) acting as zinc ligands and the gate-keeper residues present in all alpha-CAs (Glu106 and Thr199), but has a Lys in position 64 and not a His as proton shuttling residue
additional information
the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
-
the polypeptide segment Val131-Asp136 in CA IV arranges in an extended loop conformation rich of charged residues extending to the outside
additional information
the residues essential for CA2 catalytic activity are highly conserved, and also the hydrophobic portion of the CA2 active site (Val129, Val150, Leu209, Val218 and Trp220) and responsible for binding the substrate CO2 are fully conserved, active site structure
additional information
the TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure, structure comparisons, especially with human carbonic anhydrase 2, CA2, overview
additional information
three histidine residues predicted to form the Zn2+ coordination center, H233, H235, and H258, are conserved in Pl-CAN, together with four additional sites, H206, Q231, E245, and T340
additional information
-
three histidine residues predicted to form the Zn2+ coordination center, H233, H235, and H258, are conserved in Pl-CAN, together with four additional sites, H206, Q231, E245, and T340
additional information
Halalkalibacterium halodurans TSLV1
-
residues H137, H139, H156, and H110 present in the active site play an important role in catalysis, the active site of recombinant BhCA is also composed of conserved Glu and Asp acid residues
-
additional information
-
evaluation of efficiency of enzymes from Pseudomonas fragi, Micrococcus lylae, and Micrococcus luteus 2 compared to commercial Bos taurus carbonic anhydrase as biocatalysts in biomimetic sequestration of CO2 into CaCO3, the compared parameters are stability, inhibition rates by toxic metals, and pH dependency, overview. Indigenous carbonic anhydrases and their consortia exhibit enhanced CO2 sequestration competence compared to commercial bovine carbonic anhydrase
-
additional information
-
the TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure, structure comparisons, especially with human carbonic anhydrase 2, CA2, overview
-
additional information
Sulfurihydrogenibium azorense Az-Fu1 / DSM 15241 / OCM 825
-
identification of the structural features responsible for the high catalytic activity of the enzyme from Sulfurihydrogenibium azorense, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein. On the bottom of this cavity, the catalytic zinc ion is tetrahedrally coordinated by the three histidine residues (His89, His91 and His108). Enzyme SazCA active site structure and environment, important for catalytic activity, overview
-
additional information
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
structure analysis. Enzyme Cab shows significant structural differences with respect to the other enzymes of beta-class in the N-terminus, C-terminus and in the region encompassing residues 90-125. Moreover, it presents a less extended C-terminal region, being the smallest beta-CA so far characterized
-
Show AA Sequence and Transmembrane Helices (57431 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
120000
18900
-
4 * 21000, SDS-PAGE, 4 * 18900, calculated on the basis of the amino acid composition deduced from the nucleotide sequence
194000
-
gel filtration, meniscus depletion equilibrium sedimentation, analytical ultracentrifugation
21000
-
4 * 21000, SDS-PAGE, 4 * 18900, calculated on the basis of the amino acid composition deduced from the nucleotide sequence
220000
22873
22900
25000
25100
26000
27000
27500
28000
280000
recombinant enzyme CA VI-PTX, gel filtration, light scattering, and dynamic light scattering
28085
-
x * 28085, a 26-residue signal peptide is cleaved off by the Escherichia coli processing machinery, thus the recombinant enzyme has a MW of 26314 Da, calculation from nucleotide sequence
28500
29000
29300
30000
31000
32300
34000
35000
36000
37000
39000
42000
44000
50000
60000
70000
74000
79500
Halalkalibacterium halodurans
about, recombinant enzyme, gel filtration and native PAGE
80000
84000
120000
-
apparent molecular mass of the purified protein, gel filtration
22873
-
3 * 22873, determined by measuring A280S of protein solution
22900
-
or tetramer, 3 * or 4 * 22900, calculation from nucleotide sequence
22900
-
or trimer, 3 * or 4 * 22900, calculation from nucleotide sequence
27000
-
x * 27000 + x * 27500, chloroplastic isoenzyme, the two subunits are identical, except that the 27000 Da subunit is three amino acids shorter than the 27500 Da subunit, SDS-PAGE
27500
-
x * 27000 + x * 27500, chloroplastic isoenzyme, the two subunits are identical, except that the 27000 Da subunit is three amino acids shorter than the 27500 Da subunit, SDS-PAGE
29000
-
4 * 29000, SDS-PAGE, the native recombinant enzyme is a homotetramer
31000
-
3 * 31000, calculated from the log plot obtained from the relative mobility of the standard proteins in SDS-PAGE
50000
isolated recombinant detagged PG domain (PG(38-136)), gel filtration, the high retention volume observed is a consequence of a non-globular structure, PG(38-136) has an hydrodynamic dimension typical of IDPs
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotrimer
hexamer
homodimer
homotetramer
homotrimer
monomer
monomer or dimer
octamer
pentamer
5 * 58600, recombinant enzyme CA VI-PTX, SDS-PAGE, 5 * 58107, enzyme sequence without glycans and signal peptide excluded, sequence calculation
tetramer
trimer
additional information
?
x * 26000, about, recombinant optimized enzyme without signal peptide, SDS-PAGE, x * 25715, sequence calculation
?
x * 24950, sequence calculation, x * 25000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 20000, about, isolated recombinant detagged PG domain (PG(38-136)), SDS-PAGE
?
x * 37670, recombinant His-tagged enzyme, SDS-PAGE, x * 31998, sequence calculation
?
x * 36690, isozyme CA3, sequence calculation, x * 40000, SDS-PAGE
?
-
x * 28085, a 26-residue signal peptide is cleaved off by the Escherichia coli processing machinery, thus the recombinant enzyme has a MW of 26314 Da, calculation from nucleotide sequence
?
Ovis aries Kangal Akkaraman
-
x * 28890, SDS-PAGE
-
?
x * 48500, recombinant premature enzyme, SDS-PAGE, x * 46200, recombinant mature enzyme, SDS-PAGE
dimer
-
most alphaCA enzymes are monomeric, but alphaCA1 from Chlamydomonas reinhardtii is a dimer that is uniquely stabilized by disulfide bonds, crystal structure determination and analysis
dimer
enzyme CrCAH3 is a dimer at pH 4.1 that is stabilized by swapping of the N-terminal arms, a feature not previously observed in alpha-type carbonic anhydrases
dimer
-
two catalytic domains of CA IX associate to form a dimer, which is stabilized by the formation of an intermolecular disulfide bond
dimer
enzyme Cab is a dimer with the typical alpha/beta fold of beta-CAs. The two monomers within the dimer are related by a 2fold axis and their structure consists of a central beta-sheet core composed of five strands. Upon dimer formation, an extended beta-sheet core encompassing the entire dimer is formed. Several alpha-helices pack onto this beta-structural motif, resulting in a large interface area between the two enzyme subunits
dimer
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
enzyme Cab is a dimer with the typical alpha/beta fold of beta-CAs. The two monomers within the dimer are related by a 2fold axis and their structure consists of a central beta-sheet core composed of five strands. Upon dimer formation, an extended beta-sheet core encompassing the entire dimer is formed. Several alpha-helices pack onto this beta-structural motif, resulting in a large interface area between the two enzyme subunits
-
dimer
enzyme SspCA forms a dimer characterized by a large interface area and stabilized by several polar and hydrophobic interactions
hexamer
Synechocystis sp. PCC 6803 / Kazusa
enzyme CcaA shows a wellpacked trimer-of-dimers organization. The proximal part of the characteristic C-terminal extension is ordered by binding at a site that passes through the two-fold symmetry axis shared with an adjacent dimer, as a result, only one of a pair of converging termini can be ordered at any given time. beta-CA structures are organized around a tight, catalytic dimer. The catalytic site of CcaA is located at the interface between two protomers, with the zinc ion bound to Cys39, His98, and Cys101. A water molecule forms the fourth zinc ligand at pH 4.5
homodimer
Halalkalibacterium halodurans
2 * 39500, recombinant glycosylated enzyme, SDS-PAGE, 2 * 37500, recombinant deglycosylated enzyme, SDS-PAGE
homodimer
Halalkalibacterium halodurans TSLV1
-
-
-
homodimer
Halalkalibacterium halodurans TSLV1 / MTCC 10961
-
2 * 39500, recombinant glycosylated enzyme, SDS-PAGE, 2 * 37500, recombinant deglycosylated enzyme, SDS-PAGE
-
homodimer
SazCA enzyme three-dimensional structure determination and analysis, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis, PDB ID 4G7A. The SazCA monomer adopts the canonical fold of the alpha-CA family members consisting of a central ten-stranded beta-sheet surrounded by alpha- and 310-helices as well as small additional beta-sheets. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein
homodimer
Sulfurihydrogenibium azorense Az-Fu1 / DSM 15241 / OCM 825
-
SazCA enzyme three-dimensional structure determination and analysis, structure comparison with the enzyme from Sulfurihydrogenibium yellowstonensis, PDB ID 4G7A. The SazCA monomer adopts the canonical fold of the alpha-CA family members consisting of a central ten-stranded beta-sheet surrounded by alpha- and 310-helices as well as small additional beta-sheets. The active site of each monomer within the dimer is completely accessible to the solvent and, as observed for other alpha-CAs, is located in a cavity which extends from the surface to the center of the protein
-
homotetramer
-
4 * 29000, SDS-PAGE, the native recombinant enzyme is a homotetramer
homotetramer
-
4 * 29000, SDS-PAGE, the native recombinant enzyme is a homotetramer
-
homotrimer
-
3 * 31000, calculated from the log plot obtained from the relative mobility of the standard proteins in SDS-PAGE
monomer or dimer
x * 50000, native enzyme, SDS-PAGE, x * 26000, about, sequence calculation
octamer
-
x * 27000 + x * 27500, chloroplastic isoenzyme, the two subunits are identical, except that the 27000 Da subunit is three amino acids shorter than the 27500 Da subunit, SDS-PAGE
tetramer
-
recombinant Co-HICA, the crystal structure shows a four-coordinate geometry for Co-HICA with pH-dependent changes in the absorption spectrum of Co-HICA, overview
tetramer
-
or trimer, 3 * or 4 * 22900, calculation from nucleotide sequence
tetramer
-
4 * 21000, SDS-PAGE, 4 * 18900, calculated on the basis of the amino acid composition deduced from the nucleotide sequence
trimer
-
or tetramer, 3 * or 4 * 22900, calculation from nucleotide sequence
trimer
-
3 * 22873, determined by measuring A280S of protein solution
additional information
bsCA II shows pH-dependent closed or open conformation, overview
additional information
-
bsCA II shows pH-dependent closed or open conformation, overview
additional information
-
bsCA II shows pH-dependent closed or open conformation, overview
-
additional information
each unit cell is comprised of four dimers of CrCAH3
additional information
-
each unit cell is comprised of four dimers of CrCAH3
additional information
cross-sectional profiles of the gamma-CA trimer reveal that each monomer resembles an equilateral triangle, which is stabilized by hydrogen bonds, salt bridges and hydrophobic interactions. The trimer contains 3 active sites and each monomer contributes His residues located on the surface to coordinate the Zn(II) ion crucial for catalysis
additional information
-
cross-sectional profiles of the gamma-CA trimer reveal that each monomer resembles an equilateral triangle, which is stabilized by hydrogen bonds, salt bridges and hydrophobic interactions. The trimer contains 3 active sites and each monomer contributes His residues located on the surface to coordinate the Zn(II) ion crucial for catalysis
additional information
Colwellia psychrerythraea 34H / ATCC BAA-681
-
cross-sectional profiles of the gamma-CA trimer reveal that each monomer resembles an equilateral triangle, which is stabilized by hydrogen bonds, salt bridges and hydrophobic interactions. The trimer contains 3 active sites and each monomer contributes His residues located on the surface to coordinate the Zn(II) ion crucial for catalysis
-
additional information
-
overall secondary and tertiary structure of Co-HICA differ from wild-type Zn-enzyme structure, active R-state and inactive T-state conformations, overview
additional information
the studied anion binding site along the dimerization interface of HICA is an escort site that represents an intermediate along the ingress/egress route of bicarbonate ion to/from the allosteric binding site, overview. Type II beta-CAs can also adopt an active, R-state conformation in which Asp44 pairs with Arg46, allowing the coordination of the catalytically essential water molecule to the active site zinc ion. The noncatalytic bicarbonate ion stabilizes the inactive T state
additional information
-
the studied anion binding site along the dimerization interface of HICA is an escort site that represents an intermediate along the ingress/egress route of bicarbonate ion to/from the allosteric binding site, overview. Type II beta-CAs can also adopt an active, R-state conformation in which Asp44 pairs with Arg46, allowing the coordination of the catalytically essential water molecule to the active site zinc ion. The noncatalytic bicarbonate ion stabilizes the inactive T state
additional information
Halalkalibacterium halodurans
structural secondary composition of rBhCA at different pH values, overview
additional information
Halalkalibacterium halodurans TSLV1
-
structural secondary composition of rBhCA at different pH values, overview
-
additional information
-
the active form of CAIX in the MDA-MB-231 breast cancer cell line is dimeric but that neither lipid raft localization nor phosphorylation are likely required for its dimerization or activity
additional information
CA XIV is a membrane-associated glycoprotein composed of an extracellular catalytic domain, a single transmembrane helix, and a short intracellular polypeptide chain. The protein has two cysteine residues that form a disulfide bond for the stabilization of CA XIV structure and one N-glycosylation site
additional information
-
CA XIV is a membrane-associated glycoprotein composed of an extracellular catalytic domain, a single transmembrane helix, and a short intracellular polypeptide chain. The protein has two cysteine residues that form a disulfide bond for the stabilization of CA XIV structure and one N-glycosylation site
additional information
isozyme HCAII is a beta-sheet dominated monomeric protein of 259 aminoacid residues. The far-UV CD is used to characterize the intermediate states (XI and XII) for secondary structural content, near-UV CD for tertiary structure, dynamic light scatteringfor hydrodynamic radius and ANS fluorescence spectroscopy for the presence of exposed hydrophobic patches. Stable intermediates XI and XII populations of intermediates are prepared by urea-derived protein denaturation at around 2 and 4 M urea, respectively. Urea-induced XI state has characteristics ofmolten globule state while XII state bears characteristics features of pre-molten globule state, overview
additional information
-
isozyme HCAII is a beta-sheet dominated monomeric protein of 259 aminoacid residues. The far-UV CD is used to characterize the intermediate states (XI and XII) for secondary structural content, near-UV CD for tertiary structure, dynamic light scatteringfor hydrodynamic radius and ANS fluorescence spectroscopy for the presence of exposed hydrophobic patches. Stable intermediates XI and XII populations of intermediates are prepared by urea-derived protein denaturation at around 2 and 4 M urea, respectively. Urea-induced XI state has characteristics ofmolten globule state while XII state bears characteristics features of pre-molten globule state, overview
additional information
peptide mass finger prints by tryptic digestion and mass spectrometry. Secondary structure of enzyme CAVA is measured using circular dichroism. The secondary structural contents for the native CAVA include 20.2% alpha-helix, 29.1% beta-sheet and 50.7% random coil, while the renatured CAVA has 21.7% alpha-helix, 27.2% beta-sheet, and 51.3% random coil, and the denatured CAVA has 15.3% alpha-helix, 21.7% beta-sheet, and 63% random coil
additional information
-
peptide mass finger prints by tryptic digestion and mass spectrometry. Secondary structure of enzyme CAVA is measured using circular dichroism. The secondary structural contents for the native CAVA include 20.2% alpha-helix, 29.1% beta-sheet and 50.7% random coil, while the renatured CAVA has 21.7% alpha-helix, 27.2% beta-sheet, and 51.3% random coil, and the denatured CAVA has 15.3% alpha-helix, 21.7% beta-sheet, and 63% random coil
additional information
secondary structure stability of wild-type and mutant enzymes in SDS, overview
additional information
the extracellular region of the isozyme consists of the catalytic CA domain and the proteoglycan-like (PG) domain, PG domain structure determination and analysis, overview. The isolated PG domain belongs to the family of intrinsically disordered proteins, being globally unfolded with only some local residual polyproline II secondary structure, it shows conformational flexibility. Primary sequence analysis of the PG(38-136) protein, peptide analysis by gel filtration, NMR spectroscopy, and dynamic light scattering, modelling and molecular dynamics studies, overview
additional information
-
the extracellular region of the isozyme consists of the catalytic CA domain and the proteoglycan-like (PG) domain, PG domain structure determination and analysis, overview. The isolated PG domain belongs to the family of intrinsically disordered proteins, being globally unfolded with only some local residual polyproline II secondary structure, it shows conformational flexibility. Primary sequence analysis of the PG(38-136) protein, peptide analysis by gel filtration, NMR spectroscopy, and dynamic light scattering, modelling and molecular dynamics studies, overview
additional information
the dimeric enzyme TcruCA has a highly conserved yet compact structure compared with other alpha-CAs, interface structure, structure comparisons, detailed overview. The TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure
additional information
-
the dimeric enzyme TcruCA has a highly conserved yet compact structure compared with other alpha-CAs, interface structure, structure comparisons, detailed overview. The TcruCA monomer has the signature secondary structure typical of an alpha-CA fold, with helical and loop structures present towards the surface and a conical active-site cavity comprised of mostly beta-structure
-
additional information
enzyme Cab shows significant structural differences with respect to the other enzymes of beta-class in the N-terminus, C-terminus and in the region encompassing residues 90-125. Moreover, it presents a less extended C-terminal region, being the smallest beta-CA so far characterized
additional information
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
enzyme Cab shows significant structural differences with respect to the other enzymes of beta-class in the N-terminus, C-terminus and in the region encompassing residues 90-125. Moreover, it presents a less extended C-terminal region, being the smallest beta-CA so far characterized
-
additional information
in SDS-PAGE the enzyme migrates as a 66000 Da disulfide-linked dimer, which turnes into a 31000 Da monomer upon reduction with DTT
additional information
-
in SDS-PAGE the enzyme migrates as a 66000 Da disulfide-linked dimer, which turnes into a 31000 Da monomer upon reduction with DTT
additional information
in addition to the alpha-type CA-specific domain, the enzyme has a glycine-rich region at the N-terminal of the molecule functional domains
additional information
-
in addition to the alpha-type CA-specific domain, the enzyme has a glycine-rich region at the N-terminal of the molecule functional domains
additional information
the alpha-CA presents a fold characterized by a central ten-stranded beta-sheet surrounded by several helices and additional beta-strands. The active site is found in a deep conical cavity which extends from the protein surface to the center of the molecule, with the catalytic zinc ion positioned at the bottom of this cavity
additional information
CcmM is built as two distinct regions, the C-terminal region of CcmM consists of three to five repeats of a RubisCO small subunit-like domain, separated by flexible linker regions. This region binds RubisCO. The N-terminal domain is clearly homologous to gamma-CAs, but in at least some strains, including Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7942, this domain lacks measurable CA activity. CcmM's N-terminal domain is trimeric. The C-terminal end of the eta-helix is dominated by the protruding alphaA helix and the alphaA-alphaB loop
additional information
A0A2D1CFJ9
three-dimensional homology structure modeling of carbonic anhydrase VI, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phosphoprotein
proteolytic modification
side-chain modification
additional information
glycoprotein
four potentially N-glycosylated Asn residues (in the motif Asn-X-Ser/Thr) are all on the surface of the monomer
glycoprotein
Halalkalibacterium halodurans
the recombinant enzyme BhCA expressed in Pichia pastoris strain GS115 is a glycosylated protein. rBhCA possesses two potential N-glycosylation sites and many O-glycosylation sites. Enzyme deglycosylation by endoglycosylase H
glycoprotein
Halalkalibacterium halodurans TSLV1 / MTCC 10961
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the recombinant enzyme BhCA expressed in Pichia pastoris strain GS115 is a glycosylated protein. rBhCA possesses two potential N-glycosylation sites and many O-glycosylation sites. Enzyme deglycosylation by endoglycosylase H
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glycoprotein
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CAIX exists predominantly as a dimeric, high-mannose N-linked glycoprotein
glycoprotein
the HcCA3 isozyme contains four N-glycosylation sites: Asn37, Asn44, Asn195, and Asn253
glycoprotein
A0A2D1CFJ9
isozyme CA VI contains three potential N-linked glycosylation sites
phosphoprotein
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CAIX tyrosine phosphorylation in the cytoplasmic domain. EGF induces CAIX translocation to lipid rafts but not its phosphorylation
phosphoprotein
the HcCA3 isozyme contains five KinasePhos sites: Tyr24, Ser25, Ser220, Thr236, Thr249 and Ser343
proteolytic modification
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the discrepancy in molecular weight between the recombinant and the authentic enzyme suggests that the carbonic anhydrase is posttranslationally modified in either E. coli or Methanobacterium thermophilum
proteolytic modification
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a 26-residue signal peptide is cleaved off by the E. coli processing machinery
proteolytic modification
a signal peptide of 21 amino acids is identified at the N-terminal of the protein (MNAYILLSLTTLTVLYQECLG), followed by a cleavage site between the G21 and A22 residues, suggesting that Pl-CAN is a secreted protein
proteolytic modification
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ptca1 cDNA possesses a presequence of 138 bp (pre138), which encodes 46 N-terminal amino acids (Pre46AA) that does not occur in the mature PtCA1. Pre46AA is relatively rich in hydrophobic amino acids and functions as a sorting signal for PtCA1
proteolytic modification
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precursor OEC33 has a MW of 41000 Da, mature enzyme has a MW of 33000 Da
side-chain modification
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at least 20% carbohydrate, contains glucosamine, galactose and sialic acid
side-chain modification
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glycoprotein with one N-linked oligosaccharide chains, the enzyme is anchored to membrane surface by a phosphatidylinositol-glycan linkage
side-chain modification
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glutathione binding to Cys residues may have a role in the defence against oxidative damage. S-glutathionylation does not have any effect on the anhydrase activity of Ice-CA
side-chain modification
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phospholipid anchor may be acting both as an extracellular tether and as a protein activator
additional information
A0A2D1CFJ9
two cysteine residues, Cys28 and Cys209, that are likely to form one disulfide bond, are present in pufferfish CA VI
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals belong to hexagonal space group P6(1), with unit-cell parameters a : b : 66.7 A, c : 240.0 A
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X-ray absorption near edge spectroscopy (XANES)/MXAN analysis of the reaction center
purified native isozyme alphaCA1, 0.002 ml of 20 mg/ml protein in 25 mM Tris-HCl, pH 7.5, is mixed with 0.002 ml of reservoir solution, containing 1.0 M ammonium sulfate and 100 mM Tris-HCl, pH 8.5, and equilibrated against 0.7 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.88 A resolution, MAD method
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purified recombinant detagged enzyme CrCAH3 with inhibitors phosphate and acetazolamide, hanging drop vapor diffusion method, mixing of 0.001 ml of 3.6 mg/l protein in mM Tris-HCl, pH 8.0, and 150 mM NaCl, and 1 mM ligand, with 0.001 ml of reservoir solution containing 2.5 M NH4H2PO4 and 0.1 M Tris-HCl, pH 8.0, to a final pH of pH 4.1, and equilibration over 1 ml reservoir solution, at 18°C, method optimization, X-ray diffraction structure determination and analysis at 2.6-2.7 A resolution
crystal structure of dCA II at 1.86 A resolution, vapour diffusion method
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crystallized by the hanging drop vapour-diffusion method, monoclinic crystal system, crystals belong to space group P2(1), with unit-cell parameters a : 47.0 A, b : 119.9 A, c : 58.5 A
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2 different tetragonal crystal forms, form 1 space group P4(2)2(1)2, unit cell dimensions a : b : 68.54 A, c : 85.88A, form 2 space group P4(3)22, a : : b : 81.24 A, c : 162.14 A
CynT2, form 1, space group P4(2)212, unit-cell parameters a : b : 68.54 A, c : 85.88 A, form 2, space group P4(3)22, a : b : 81.00 A, c : 161.98 A, form 3, space group P2(1), a : 48.21, b : 140.73, c : 72.57, selenomethionine-substituted crystals, space group P4(3)22, a : b : 81.24 A, c : 162.14 A
purified recombinant Co-HICA by hanging drop vapor diffusion, 10 mg/ml protein crystallized in 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.5, 0.1 M (NH4)2SO4, and 27% PEG 4000, 22°C, several days, X-ray diffraction structure determination and analysis at 2.5 A resolution
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purified wild-type and mutant enzymes, 12 mg/ml protein mixed with 0.7 M sodium potassium tartrate, 0.10 M HEPES, pH 7.5, for tetragonal crystals and with 1.8 M ammonium sulfate, 4% PEG 400, 0.10 M HEPES, pH 7.5, for monoclinic crystals, 22°C, 2-3 days, crystals are soaked for 1-2 min in artificial mother liquor plus either 30% glucose or 30% glucose and 100 mM NaHCO3, X-ray diffraction structure determination and analysis
hanging drop vapor diffusion method. 2.2 A crystal structure of CsoSCA
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all variants crystallized in the orthorhombic P2(1) 2(1) 2 (1) space group and are highly isomorphous with approximate unit cell dimensions a=42, b=72 and c=75 A and diffract between 1.56 and 2.0 A resolution
CA XII crystallized by the hanging drop vapor diffusion method, space group C2 with unit cell dimensions a : 146.7 A, b : 44.6 A, c : 85.2 A
carbonic anhydrase II complexed with two aromatic sulfonamide inhibitors N-(4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide and N-(2-fluoro-4-sulfamoylphenyl)-2-(thiophen-2-yl)acetamide incorporating 2-thienylacetamido moieties, hanging drop vapor diffusion method, drops of 0.005 ml containing 0.5 mM hCA II, 1 mM inhibitor, 0.1% DMSO, 0.8 M sodium citrate, 50 mM Tris-HCl, pH 8.0,are equilibrated against 1 ml precipitant solution containing 1.6 M sodium citrate and 50 mM Tris-HCl, pH 8.0, at room temperature, X-ray diffraction structure determination and analysis at 1.6-1.7 A resolution
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crystal structure of the hCA II/2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide adduct
crystal structure of the hCA/2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide adduct
crystal structures of C-terminal hexahistidine-tagged carbonic anhydrase III and F198L carbonic anhydrase III, hanging-drop vapour diffusion method, 2.1 A resolution
crystals obtained by hanging drop technique, hCA II-sulfamate, space group P2(1), a : 42.32 A, b : 41.48 A, c : 72.44 A, hCA II-sulfamide, space group P2(1), a : 42.70 A, b : 41.70 A, c : 73.00 A
crystals obtained by hanging drop technique, space group P2(1), cell parameters a: 42.01 A, b : 41.43 A, c: 71.99 A
crystals obtained using the hanging drop vapor diffusion method, isozyme CA I Michigan I, space group P2(1)2(1)2(1), with unit cell dimensions parameters a : 62.50 A, b : 72.13 A, c : 121.54 A, isozyme CA I Michigan 1-Zn(II)2, space group P2(1)2(1)2(1), with unit cell dimensions parameters a : 62.68 A, b : 71.36 A, c : 120.91A
crystals of carbonic anhydrase II and carbonic anhydrase IX mimic are grown at room temperature using the hanging drop vapour diffusion method
crystals of K64H, R67H, and K64H/R67N HCA III are grown by hanging drop vapor diffusion method. X-ray crystal structures of site-specific mutants of human carbonic anhydrase III (HCA III): K64H, R67H, and K64H/R67N HCA III
crystals of the HCA II single-site mutants Y7F, N62L, and N67L are obtained using the hanging-drop vapor diffusion method. All crystals are isomorphous and belong to space group P2(1) with mean unit cell dimensions: a = 42.7 A, b = 41.6 A, c = 72.9 A and beta = 104.6°
hanging drop vapor diffusion method, using 0.4 M NH4H2PO4, 0.1 M sodium citrate, pH 5.0
holoenzyme and apoenzyme are crystallized by hanging drop vapour diffusion method, using 1.3 M sodium citrate, 100 mM Tris-HCl, pH 7.8
in complex with inhibitor RWJ-37497, crystals obtained by the hanging-drop vapour-diffusion method, space group P2(1) with unit cell parameters a : 42.28 A, b : 41.39 A, c : 72.51 A
isoform CA II in complex with 6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide, hanging drop vapor diffusion method, using 2.5 M (NH4)2SO4, 0.3 M NaCl, 100 mM Tris-Cl, pH 8.2
isoform CA II, sitting drop vapor diffusion method, using 0.1 M sodium bicine, 0.2 M ammonium sulfate and 2 M sodium malonate
isozyme CA XIII in the unbound state and in complex with acetazolamide, hanging drop vapour diffusion method, in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 1 mM dithiothreitol with 30% (w/v) polyethylene glycol 4000, 0.2 M ammonium acetate, 0.1 M sodium acetate, pH 4.6
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mutant H64A, crystals produced by the hanging drop method, space group P2(1) with unit cell parameters of a : 42.5 A, b : 41.6 A, c : 72.7 A
mutants are crystallized by hanging drop vapour diffusion method, with 50 mM Tris-HCl (pH 9.0) and 1.3 M sodium citrate at 20°C
purified enzyme in complex with inhibitors (S)-4-(4-acetyl-3-benzylpiperazine-1-carbonyl)benzene-1-sulfonamide and (S)-4-[2-benzyl-4-(4-sulfamoylbenzoyl)piperazine-1-carbonyl]benzene-1-sulfonamide, sitting drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 9.0, with 0.002 ml of a solution of 28-31% PEG 4000, 0.2 M sodium acetate, 0.1 M Tris, pH 8.5-9.0 and equilibration against the same solution at 23°C, fifteen days, afterwards the crystals are soaked in 5 mM inhibitor solutions for 3 days, X-ray diffraction structure determination and analysis at 1.5-1.6 A resolution
purified isozyme CA II (chimeric CA IX mimic) mutant in complex with inhibitors 4-phenylbenzene-1-sulfonamide, 4-(2-methylphenyl)benzene-1-sulfonamide, 4-(3-formylphenyl)benzene-1-sulfonamide, and 4-(3-quinolinyl)benzene-1-sulfonamide, sitting drop vapor diffusion method, mixing of 300-500 nl of 20 mg/mL of CA II and 41 mg/ml of the CA IX mimic solution with crystallization solution containing 1.6 M sodium citrate, 50 mM Tris-HCl, pH 7.8, in a ratio of 3:5 or 1:1, 25°C, 1 week, X-ray diffraction structure determination and analysis at 1.55-1.69 A resolution (PDB IDS 5SZ0, 5SZ1, 5SZ2, and 5SZ3), molecular replacement using the enzyme structure PBD ID 3KS3 without zinc and solvent as search model
purified isozyme CA IX in complex with inhibitors 4-phenylbenzene-1-sulfonamide, 4-(2-methylphenyl)benzene-1-sulfonamide, 4-(3-formylphenyl)benzene-1-sulfonamide, and 4-(3-quinolinyl)benzene-1-sulfonamide, X-ray diffraction structure determination and analysis at 1.15-1.78 A resolution (PDB IDS 5SZ4, 5SZ5, 5SZ6, and 5SZ7), molecular replacement using the enzyme structure PBD ID 3KS3 without zinc and solvent as search model
purified recombinant differently isotope-labeled isozyme hCAII, 14 mg/ml protein, both vapour diffusion and microbatch under-oil techniques are valuated, hanging and sitting drop set-ups with 0.01 ml drops, microseeding, deuteration of hCA II does not affect the crystal structure. Large, single crystals grow for both H and D enzyme versions in microbatch under-oil experiments at pH 8.5, room temperature, X-ray diffraction structure determination and analysis
purified recombinant differently isotope-labeled isozyme hCAIX, 17 mg/ml protein, both vapour diffusion and microbatch under-oil techniques are valuated, hanging and sitting drop set-ups with 0.01 ml drops, microseeding, room temperature, deuteration of hCA XI does not affect the crystal structure, but for D-hCA IX mimic no crystals appear in any of the under-oil batch trays at all pHs tested, while H-hCA IX SV gives several good crystals per drop at pH 8.5. X-ray diffraction structure determination and analysis
purified recombinant HCA II, crystals are prepared at pH 6.0, pH 8.5, and pH 11.0, hanging drop vapor diffusion method, crystal preparation from apo-Co(II)-HCA II by mixing 0.005 ml of protein solution with 0.005 ml of precipitant solution, containing 1.4 M sodium citrate, and 100 mM Tris-HCl, pH 9.0, at room temperature, and soaking of the crystals in 100 mM CoCl2, 1.4 M sodium citrate, 50 mM Tris-Cl, 50 mM 3-(cyclohexylamino)propanesulfonic acid with pH values of 6.0, 8.5 and 11.0, respectively, 2-3days, X-ray diffraction structure determination and analysis at 1.5-1.6 A resolution
purified recombinant human CA II in complex with imidazole-based activator CAA12i, hanging drop vapor diffusion method, mixing of 10 mg/ml protein and 0.2 mM ligand in 50 mM Tris-HCl, pH 7.8, with reservoir solution, containing 50 mM Tris HCl and 1.3 M sodium citrate, pH 7.4, in a 1:1 ratio, 23°C, 7 days without agitation, X-ray diffraction structure determination and analysis at 1.6 A resolution
purified recombinant K170 HCA II variants, hanging drop vapour diffusion method, 2-3days, X-ray diffraction structure determination at room temperature and analysis
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purified recombinant wild-type enzyme and mutants M1-M4, X-ray diffraction structure determination and analysis at resolutions of 1.62-2.29 A
site-specific mutant Y7H, crystals produced by the hanging drop method, space group P2(1) with unit cell dimensions a : 42.9 A, b: 41.6 A, c : 73.0 A
sitting drop vapor diffusion method, using 10% (w/v) PEG 6000, 0.3 M NH4Cl pH 6.3, and 10% (v/v) ethylene glycol
the hCA II-sulthiame complex is crystallized by cocrystallization procedures. High resolution crystal structure of the hCA II-sulthiame adduct
the hCA IIN-hydroxysulfamide complex is cocrystallized at 4°C by the hanging drop vapor diffusion method. X-ray crystal structure of the human hCA II-N-hydroxysulfamide adduct
X-ray absorption nearedge spectroscopy (XANES)/MXAN analysis of the reaction center
X-ray crystallographic structure of the disulfide-containing HCAII (dsHCAII) is solved to 1.77 A resolution
purified recombinant enzyme, sitting drop vapour diffusion, using a precipitant solution consisting of 2% v/v Tacsimate, pH 4.0, 0.1 M sodium acetate trihydrate, pH 4.6, and 16% w/v PEG 3350, 10 days at 17°C, X-ray diffraction structure determination and analysis at 2.6 A resolution
cubic crystals, space group P2(1)3, Zn-Cam, unit cell a : b : c: 82.64 A, Zn-Cam-HCO3-, unit cell a : b : c: 82.51 A, Zn-Cam-SO42-, unit cell a : b : c: 82.68 A, Co-Cam, unit cell a : b : c: 82.34 A, Co-Cam-HCO3-, unit cell a : b : c: 82.58 A, Co-Cam-SO42-, unit cell a : b : c: 82.61 A
purified enzyme in complex with Zn2+ and Co2+, X-ray diffraction structure determination and analysis, PDB ID 1QRG
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the crystal structure of the enzyme is determined at 2.8 A resolution using the method of multiple isomorphous replacement in combination with 3fold non-crystallographic symmetry averaging and phase extension
crystals grown by hanging drop method, orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a : 54.9 A, b : 113.2 A, c : 156.2 A
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enzyme crystal structure determination and analysis, Cab dimer, PDB ID 1G5C
crystallized by hanging drop vapor diffusion method, crystals belong to space group P2(1) with unit cell dimesions a : 59.0 A, b : 75.6 A, c : 73.2 A
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crystallized by the vapor diffusion method, hanging drop, space group C2, unit cell parameters a : 99.3 A, b : 66.7 A, c : 92.6 A
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structure of the extracellular domain of murine CA XIV solved at 2.8 A resolution, and the enzyme-acetazolamide complex at 2.9 A resolution
in complex with the inhibitor acetic acid, crystals of the orthorhombic space group C222 with cell parameters a : 136.9 A, b : 143.3 A, c : 202.1 A
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in complex with Ca2+, sitting drop vapour diffusion method, with 22.5% PEG 4000 in MES-NaOH pH 5.8 and 0.1 M lithium chloride as the precipitating agent
Nce103 in complex with a substrate analog at 2.04 A resolution, hanging drop vapor diffusion method, using 20% (w/v) PEG4000, 0.1 M sodium citrate, pH 5.6, 0.1 M sodium acetate, 20% (v/v) ethylene glycol, at 16°C
purified recombinant His-tagged enzyme incomplex with inhibitor acetazolamide, hanging drop vapor diffusion method, mixing of 0.001 ml of 8 mg/ml protein in 20 mM Tris, pH 8.3, and a 10-molar excess of the inhibitor with 0.001 m of reservoir solution containing 30% w/v PEG monomethyl ether 550, 0.05 M MgCl2, and 0.1 M HEPES, pH 7.5, and equilibration against 0.5 ml of reservoir solution, 1 week, room temperature, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement using the structure of enzyme SspCA from Sulfurihydrogenibium yellowstonensis (PDB ID 4G7A) as a search model
purified enzyme in complex with inhibitor acetazolamide, X-ray diffraction structure determination and analysis, PDB ID 4G7A
purified recombinant truncated enzyme CcaA220, by sitting drop vapor diffusion method, mixing of 0.001 ml of 7 mg/ml protein solution with 0.001 ml of well solution containing 2.0 M Na formate and 0.1 M Na acetate, pH 4.6, X-ray diffraction structure determination and analysis at 1.45 A resolution, molecular replacement using the structure of a catalytic dimer (residues 121-318) from Pisum sativum beta-CA (PDB ID 1ekj) as a search model
Synechocystis sp. PCC 6803 / Kazusa
vapor diffusion method, using 1.0 M ammonium sulfate, 0.1 M [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)methane, 1% (w/v) PEG 3350, pH 5.5
Thermosynechococcus vestitus
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H216N
H64A
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shuttling mutant CAII-H64A shows lower catalytic activity compared to wild-type. Mutant displays catalytic activity in intact oocytes, also reduces the SNAT3-associated membrane conductance, when glutamine, but not when asparagine is the substrate
G41A
the mutant has kcat/Km values similar to wild-type enzyme, and exhibits a similar dramatic decrease in catalytic activity at pH values below pH 8.0, but HICA-G41A is serendipitously found to bind sulfate ion or bicarbonate ion near pairs of Glu50 and Arg64 residues located on the dimerization interface, 2 of 12 chains in the asymmetric unit bind bicarbonate ion exclusively at the dimerization interface, while the remaining 10 chains bind bicarbonate ion exclusively at the allosteric site
V47A
the mutant has kcat/Km values similar to wild-type enzyme, and exhibits a similar dramatic decrease in catalytic activity at pH values below pH 8.0, but HICA-V47A is serendipitously found to bind sulfate ion or bicarbonate ion near pairs of Glu50 and Arg64 residues located on the dimerization interface, bicarbonate ions simultaneously bind to both the dimerization interface and the allosteric sites
A23C/L203C/C206S
mutant retains high catalytic efficiency, and differential scanning calorimetry shows acid stability and thermal stability that is enhanced compared with native enzyme
A65L
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site-specific mutagenesis, enhancement of activity with all substrates, about 5fold increase in activity with 4-nitrophenyl acetate
A65L/T200G
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site-specific mutagenesis, 5fold increase in activity with 4-nitrophenylacetate
A65L/T200R
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site-specific mutagenesis, 4fold increase in activity with 4-nitrophenylacetate
A65S
the mutation can cause variations in binding affinity of small molecule inhibitors
A65S/N67Q/E69T/I91L/F131V/K170E/L204A
site-directed mutagenesis, active site mutant
C183S/C188S
mutations at positions 183 and 188 are to enhance crystallization by removing oxidizable cysteine residues. The positions of residues 183 and 188 are solvent exposed on the side of the enzyme opposite to the active site. The mutations C183S and C188S do not affect catalysis
E234P
site-directed mutagenesis, residue Glu234, which is positioned in a surface loop, is substituted with a proline residue. Thermal stability analysis of this variant indicates an enhanced melting temperature of about 3°C compared to the wild-type enzyme
F198L/C183S/C188S
the ratio of turnover-number to Km-value for hydration of CO2 of mutant enzyme F198L/C183S/C188S is 25fold higher than the ratio of wild-type enzyme and mutant enzyme C183S/C188S
G8D/K18E/N24D/K36D/V39D/V50D/R57D/N62D/Q74E/T85D/Q136E/K169E/N177D/N186E/Q220E/L238E/N252D/Q254E
site-directed mutagenesis, mutant M4, shows reduced activity but increased thermostability and halostability compared to wild-type enzyme. The successful redesign of a mesohalophile enzyme to an extremely halotolerant orthologue, that is, one that is active at 3M NaCl and above. Role of Na+ in stabilizing M4 structure, molecular dynamics simulations, overview
G8D/K36D/V50D/N62D/Q136E/L238E
site-directed mutagenesis, mutant M2, shows reduced activity but increased thermostability and halostability compared to wild-type enzyme
G8D/N24D/K36D/V39D/V50D/R57D/N62D/Q74E/Q136E/K169E/L238E/N252D
site-directed mutagenesis, mutant M3, shows reduced activity but increased thermostability compared to wild-type enzyme
H64A
H67R
site-directed mutagenesis, single point mutation in a critical region of the active site
K170A
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site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II
K170D
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site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II
K170E
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site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II
K170H
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site-directed mutagenesis, the active site residue K170 is located near the side chain of His64, but over 15 A away from the active site zinc. The mutation leads to His64 inward conformation associated with a decrease in the pKa of His64 and an increase in the rate constant for proton transfer compared to the wild-type HCA II
K64H
K64H/R67N
mutant has enhanced proton transfer in catalysis compared with wild-type HCA III
L100H/L224S/L240P
kcat/Km (CO2) decreased compared to wild-type, T(M): 65°C compared to wild-type: 58°C, T (inactivation): 65°C compared to wild-type: 60°C
L100H/L224S/L240P/Y7F
kcat/Km (CO2) slightly decreased compared to wild-type, T(M): 61.1°C compared to wild-type: 58°C, T (inactivation): 65°C compared to wild-type: 60°C
L100H/L224S/L240P/Y7F/N62L
kcat/Km (CO2) decreased compared to wild-type, T(M): 58.1°C compared to wild-type: 58°C, T (inactivation): 60°C compared to wild-type: 60°C
L100H/L224S/L240P/Y7F/N62L/N67Q
kcat/Km (CO2) slightly decreased compared to wild-type, T(M): 59.2°C compared to wild-type: 58°C, T (inactivation): 60°C compared to wild-type: 60°C
L100H/L224S/L240P/Y7F/N67Q
kcat/Km (CO2) decreased compared to wild-type, T(M): 62.7°C compared to wild-type: 58°C, T (inactivation): 65°C compared to wild-type: 60°C
L198A
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site-specific mutagenesis, 5fold decrease in activity with 4-nitrophenylacetate
L204S
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affinity for sulfonamides/sulfamate inhibitor is moderately decreased compared to wild-type. kcat and Km (CO2) comparable to wild-type
N24D/V39D/R57D/Q74E/K169E/N252D
site-directed mutagenesis, mutant M3, shows reduced activity but increased thermostability and halostability compared to wild-type enzyme
N62A
the mutant shows a predominantly inward orientation of the side chain of His64
N62D
N62L
the mutant shows a predominantly inward orientation of the side chain of His64
N62T
the mutant shows both inward and outward orientation of the side chain of His64 like the wild type enzyme
N62V
the mutant shows a predominantly inward orientation of the side chain of His64
N67I
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affinity for sulfonamides/sulfamate inhibitor is highly decreased compared to wild-type. kcat and Km (CO2) comparable to wild-type
N67L
N67Q
the mutation can cause variations in binding affinity of small molecule inhibitors
Q92V
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affinity for sulfonamides/sulfamate inhibitor is decreased compared to wild-type. kcat and Km (CO2) comparable to wild-type
R67H
R67N
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mutant of carbonic anhydrase III, pH-dependent behavior and enhanced CO2 hydration activity compared to the wild-type enzyme, no enhanced hydrolysis rate
T200A
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site-specific mutagenesis, enhancement of activity with all substrates, about 2fold increase in activity with 4-nitrophenyl acetate
T200D
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site-specific mutagenesis, 93fold decrease in activity with 4-nitrophenylacetate
T200G
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site-specific mutagenesis, 3fold increase in activity with 4-nitrophenyl acetate
T200H
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site-specific mutagenesis, enhancement of activity with all substrates, 2fold increase in activity with 4-nitrophenyl acetate
T200I
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site-specific mutagenesis, enhancement of activity with all substrates, 1.5fold increase in activity with 4-nitrophenyl acetate
T200K
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site-specific mutagenesis, enhancement of activity with all substrates, 1.3fold increase in activity with 4-nitrophenyl acetate
T200R
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site-specific mutagenesis, enhancement of activity with all substrates, 7fold increase in activity with 4-nitrophenyl acetate
T200S
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site-specific mutagenesis, 3fold increase in activity with 4-nitrophenyl acetate, decrease in activity with all other substrates
V121A
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site-specific mutagenesis, 4fold decrease in activity with 4-nitrophenylacetate
V143A
V143G
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site-specific mutagenesis, 6fold decrease in activity with 4-nitrophenylacetate
V207A
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site-specific mutagenesis, 1.5fold decrease in activity with 4-nitrophenylacetate
V62H/H67N/H200T
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complex effect on the catalytic and inhibitor-binding properties
Y7F
Y7F/T200G
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site-specific mutagenesis, 1.5fold increase in activity with 4-nitrophenylacetate
Y7F/T200R
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site-specific mutagenesis, 7.5fold increase in activity with 4-nitrophenylacetate
Y7H
Y7I
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site-directed mutagenesis, replacement of Tyr7 with Ile has no effect on the interconversion of bicarbonate and CO2, but enhances intramolecular proton transfer approximately twofold. No changes occur in the ordered solvent structure in the active-site cavity or in the conformation of the side chain of the proton shuttle His64, while the first 11 residues of the amino-terminal chain in Y7I HCA II assume an alternate conformation compared to the wild-type enzyme
C148S
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the mutation eliminate potential problems with the oxidation of the single cysteine residue at position 148
E84 A
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site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 C
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site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 D
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site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 H
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site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 K
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 Q
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 S
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84 Y
-
site-directed mutagenesis, large decrease in kcat values in pH 7.5 MOPS buffer
E84A
-
proton shuttle replaced with a residue that does not transfer protons
W19A
kcat/km at pH 7.5 is 2.5fold lower than wild-type value, kcat/km at pH 8.8 is 2.2fold lower than wild-type value
W19F
kcat/km at pH 7.5 is 5fold lower than wild-type value, kcat/km at pH 8.8 is 5.2fold lower than wild-type value
W19N
kcat/km at pH 7.5 is 3.2fold lower than wild-type value, kcat/km at pH 8.8 is 2.4fold lower than wild-type value
Y200A
kcat/km at pH 7.5 is 3.5fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value
Y200F
kcat/km at pH 7.5 is 3.6fold higher than wild-type value, kcat/km at pH 8.8 is 2.5fold lower than wild-type value
Y200S
kcat/km at pH 7.5 is 3fold higher than wild-type value, kcat/km at pH 8.8 is 3.3fold higher than wild-type value
F65A/Y131C
-
covalently modified at cysteine residues with 4-chloromethylimidazole, exhibits an up to 3fold enhancement of catalytic activity over that of wild-type
R117H
-
site-directed mutagenesis, replacement reconstructs a zinc-binding site and changes a catalytically inactive murine carbonic anhydrase-related protein to an active carbonic anhydrase
R94H
-
site-directed mutagenesis, replacement reconstructs a zinc-binding site and changes a catalytically inactive murine carbonic anhydrase-related protein to an active carbonic anhydrase
Y64H/F65A
-
CAV variant, double mutation, transforms CAVeffectively into an anlogue of CAII, the prototypical carbonic anhydrase isozyme
H66A
-
higher sensitivity to inhibitor 6-ethoxy-2-benzo-thiazolesulfonamide
E276A
-
somewhat defective in catalytic activity, to varying degrees in different buffers. 40% of wild-type activity in HEPES/KOH buffer, 77.5% of wild-type activity in imidazole buffer, 6% of wild-type activity in HEPES/KOH buffer
H208A
-
site-directed mutagenesis, mutant is more easily inactivated by oxidation than the wild-type enzyme
H209N
-
somewhat defective in catalytic activity, to varying degrees in different buffers, 44% of wild-type activity in imidazole buffer
additional information
H216N
-
proton shuttle replaced with a residue that does not transfer protons
K64H
-
mutant of carbonic anhydrase III, pH-dependent behavior and enhanced CO2 hydration activity compared to the wild-type enzyme, no enhanced hydrolysis rate
K64H
mutant has enhanced proton transfer in catalysis compared with wild-type HCA III
N62D
the mutant shows a predominantly outward orientation of the side chain of His64
N67L
turnover-number for hydration is 1.4fold lower than wild-type value. Turnover-number for dehydration is 5.8fold lower than wild-type value
N67L
the hydrogen-bonding network is disruptedin the active site of the N67L mutant, shows inability to stabilize water clusters when His64 is in the inward orientation, thereby favoring proton transfer when His64 is in the outward orientation
R67H
mutant has enhanced proton transfer in catalysis compared with wild-type HCA III
V143A
-
site-specific mutagenesis, 2fold decrease in activity with 4-nitrophenylacetate
Y7F
turnover-number for hydration is identical to wild-type value. Turnover-number for dehydration is 5.8fold lower than wild-type value
Y7F
the mutation has the effect of increasing the proton transfer rate by 7fold in the dehydration direction of the enzyme reaction compared to the wild type enzyme
Y7F
kcat/Km (CO2) equal to wild-type, T(M): 53°C compared to wild-type: 58°C
additional information
design of a mature form ofASCA(mASCA) using a codon optimization of ASCA gene and removal of the ASCA signal peptide. mASCA is highly expressed and highly stable. The recombinant engineered enzyme ASCA can promote CO2 absorption in an alkaline solvent required for efficient carbon capture
additional information
-
design of a mature form ofASCA(mASCA) using a codon optimization of ASCA gene and removal of the ASCA signal peptide. mASCA is highly expressed and highly stable. The recombinant engineered enzyme ASCA can promote CO2 absorption in an alkaline solvent required for efficient carbon capture
additional information
-
RNAi by feeding is performed on wild-type worms for all genes, silencing of genes cah-3 and cah-4 reduces the life-span of the worms at 22°C, phenotypes, overview
additional information
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
additional information
-
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
additional information
Caminibacter sp.
-
development and the kinetic characterization of a solid CA-based biocatalyst to be used in CO2 capture processes based on reactive absorption. The commercially availbale technical grade thermostable CA is immobilized by covalent bonding on aminated paramagnetic Fe3O4 nanoparticles via carbodiimide activation of the enzyme. The effective covalent binding of the enzyme on the support is verified in the alkaline carbonate solution used as solvent for CO2 absorption tests. The kinetics of the biocatalyst are assessed by means of CO2 absorption tests in a stirred cell reactor. The liquid solvents used in the CO2 absorption tests are 0.5 M Na2CO3/NaHCO3 buffer, pH 9.6, at 25°C and 40°C and 10% w/w K2CO3 solutions at different carbonate conversion degrees (0-40%). Intrinsic second order kinetic constant kcat/KM for the CO2 hydration reaction catalyzed by the immobilized CA and method validation
additional information
generation of a CrCIA3 deletion mutant. Point mutations A399C, C499G, C525G, A570G, G732C, G888C, and C903G, none of these mutations introduces changes in the CrCAH3 amino acid sequence
additional information
-
generation of a CrCIA3 deletion mutant. Point mutations A399C, C499G, C525G, A570G, G732C, G888C, and C903G, none of these mutations introduces changes in the CrCAH3 amino acid sequence
additional information
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
additional information
knockdown of gene ca6 via two different antisense gene ca6-morpholino oligonucleotides-injected larvae. Zebrafish cannot swim properly in the ca6 knockdown model, in underdeveloped or deflated swim bladder in ca6 morphant larvae is observed, swimming pattern analysis of ca6 morphant and wild-type zebrafish, phenotype, overview
additional information
-
knockdown of gene ca6 via two different antisense gene ca6-morpholino oligonucleotides-injected larvae. Zebrafish cannot swim properly in the ca6 knockdown model, in underdeveloped or deflated swim bladder in ca6 morphant larvae is observed, swimming pattern analysis of ca6 morphant and wild-type zebrafish, phenotype, overview
additional information
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
additional information
Desulfovibrio vulgaris Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303
-
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
additional information
Halalkalibacterium halodurans
the recombinant enzyme expressed from Pichia pastoris has a higher thermostability, a higher molecular weight and is glycosylated, as compared the unglycosylated recombinant enzyme expressed from Escherichia coli, overview
additional information
Halalkalibacterium halodurans TSLV1 / MTCC 10961
-
the recombinant enzyme expressed from Pichia pastoris has a higher thermostability, a higher molecular weight and is glycosylated, as compared the unglycosylated recombinant enzyme expressed from Escherichia coli, overview
-
additional information
-
replacement of Tyr7 with eight other amino acids has no effect on the interconversion of bicarbonate and CO2, but in some cases causes enhancements in the rate constant of proton transfer by nearly 10fold. Mutant variants at position 7 show a melting temperature approximately 8°C lower than that of the wild-type enzyme
additional information
construction of a chimeric enzyme, the mimic is a chimeric protein of CA II containing seven active-site-residue mutations to resemble CA IX, allowing for ease of protein expression and crystallization. The active-site mutations, A65S, N67Q, E69T, I91L, F131V, K170E, L204A, result in approximately 90% sequence homology between the mimic and wild-type CA IX active sites, such that drugs bound to the CA IXb mimic are representative of the interactions that occur with the wild type enzyme
additional information
construction of a chimeric enzyme, the mimic is a chimeric protein of CA II containing seven active-site-residue mutations to resemble CA IX, allowing for ease of protein expression and crystallization. The active-site mutations, A65S, N67Q, E69T, I91L, F131V, K170E, L204A, result in approximately 90% sequence homology between the mimic and wild-type CA IX active sites, such that drugs bound to the CA IXb mimic are representative of the interactions that occur with the wild type enzyme
additional information
construction of a chimeric enzyme, the mimic is a chimeric protein of CA II containing seven active-site-residue mutations to resemble CA IX, allowing for ease of protein expression and crystallization. The active-site mutations, A65S, N67Q, E69T, I91L, F131V, K170E, L204A, result in approximately 90% sequence homology between the mimic and wild-type CA IX active sites, such that drugs bound to the CA IXb mimic are representative of the interactions that occur with the wild type enzyme
additional information
construction of a chimeric enzyme, the mimic is a chimeric protein of CA II containing seven active-site-residue mutations to resemble CA IX, allowing for ease of protein expression and crystallization. The active-site mutations, A65S, N67Q, E69T, I91L, F131V, K170E, L204A, result in approximately 90% sequence homology between the mimic and wild-type CA IX active sites, such that drugs bound to the CA IXb mimic are representative of the interactions that occur with the wild type enzyme
additional information
enzyme immobilization on magnetic nanoparticles (MNPs) by co-precipitation method. Silica coating with tetraethyl orthosilicate and amine functionalization of silica coated MNPs by using 3-aminopropyltriethoxysilane are performed. After activation with glutaraldehyde of silica coated MNPs, human carbonic anhydrase (hCA I) is immobilized on silica coated MNPs. Characterization of nanoparticles by transmission electron microscopy, fourier transform infrared spectroscopy, X-ray powder diffraction, and vibrating sample magnetometer. Method evaluation and optimization with respecto to activity, kinetic parameters (Km, Vmax, kcat, kcat/Km), thermal stability, storage stability and reusability of immobilized enzyme, overview. The immobilized hCA I possesses a better thermal stability than free hCA I at 30-50°C. After 40 days storage, the free hCA I sustains 50% and 0.11% of its original activity, whereas the immobilized hCA I retains 89% and 85% of its original activity at 4°C and 25°C, respectively. The immobilized hCA I retains 61% of its initial activity after successively utilization for 13 cycles
additional information
halotolerance can be generated in an enzyme solely by modifying surface residues. Rational design of carbonic anhydrase II is undertaken in three stages replacing 18 residues in total, crystal structures confirm changes are confined to surface residues. Catalytic activities and thermal unfolding temperatures of the designed enzymes increase at high salt concentrations demonstrating their shift to halotolerance, whereas the opposite response is found in the wild-type enzyme. Molecular dynamics calculations, overview
additional information
optimization of expression media and cell culture conditions to produce high levels of 3 different deuterated human carbonic anhydrases (hCAs). The labeled hCAs are then characterized and tested for deuterium incorporation by mass spectrometry, temperature stability, and propensity to crystallize, overview. Deuteration highly reduces the enzyme yield
additional information
optimization of expression media and cell culture conditions to produce high levels of 3 different deuterated human carbonic anhydrases (hCAs). The labeled hCAs are then characterized and tested for deuterium incorporation by mass spectrometry, temperature stability, and propensity to crystallize, overview. Deuteration highly reduces the enzyme yield
additional information
-
optimization of expression media and cell culture conditions to produce high levels of 3 different deuterated human carbonic anhydrases (hCAs). The labeled hCAs are then characterized and tested for deuterium incorporation by mass spectrometry, temperature stability, and propensity to crystallize, overview. Deuteration highly reduces the enzyme yield
additional information
optimization of expression media and cell culture conditions to produce high levels of 3 different deuterated human carbonic anhydrases (hCAs). The labeled hCAs are then characterized and tested for deuterium incorporation by mass spectrometry, temperature stability, and propensity to crystallize, overview. The protein appears to be more temperature stable at pH 7.5-8.5 compared to pH 5.5
additional information
optimization of expression media and cell culture conditions to produce high levels of 3 different deuterated human carbonic anhydrases (hCAs). The labeled hCAs are then characterized and tested for deuterium incorporation by mass spectrometry, temperature stability, and propensity to crystallize, overview. The protein appears to be more temperature stable at pH 7.5-8.5 compared to pH 5.5
additional information
-
optimization of expression media and cell culture conditions to produce high levels of 3 different deuterated human carbonic anhydrases (hCAs). The labeled hCAs are then characterized and tested for deuterium incorporation by mass spectrometry, temperature stability, and propensity to crystallize, overview. The protein appears to be more temperature stable at pH 7.5-8.5 compared to pH 5.5
additional information
-
polyhemoglobin-superoxide dismutase-catalase-carbonic anhydrase, poly-[SFHb-SOD-CAT-CA], is a constructed type of blood substitute. The enzymes polyhemoglobin, superoxide dismutase, catalase, and carbonic anhydrase (SFHb, SOD, CAT, CA) are all cross-linked together to form a nano-sized soluble blood substitute. The enzymes activities of the freeze-dried cross-linked enzyme complex poly-[SFHb-SOD-CAT-CA] are more stable compared with the soluble poly-[SFHb-SOD-CAT-CA] and even more so when compared to the uncrosslinked solution of free SFHb, SOD, CAT and CA enzymes
additional information
substitution in hCA II of residues 23 and 203 with two cysteines (dsHCA II) to reproduce a disulfide bridge conserved in many members of alpha-CA class. Thermal stability investigations of this variant shows that the melting temperature is enhanced by 14°C compared to the wild-type enzyme, while the catalytic efficiency is similar to that of native enzyme
additional information
although Trp19 and Y200 are non-essential, they contribute to an extended active-site structure distant from the catalytic metal that fine tunes catalysis. Trp19 is important for both CO2/bicarbonate interconversion, and the proton transfer step of catalysis
additional information
-
although Trp19 and Y200 are non-essential, they contribute to an extended active-site structure distant from the catalytic metal that fine tunes catalysis. Trp19 is important for both CO2/bicarbonate interconversion, and the proton transfer step of catalysis
additional information
-
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview. Immobilizing the enzyme within solid supports improves the method. Formation of gamma-CA nanoassemblies, where individual enzymes are connected to each other and make multiple linked interactions with the reactor surface. This can be achieved by mutating specific enzyme residues to cysteines, in order to introduce sites for biotinylation, thus allowing the subsequent formation of stable nanostructures by cross-linking of biotinylated-gamma-CAs with streptavidin tetramers. Further addition of an immobilization sequence at amino- or carboxy-terminus also allows for a controlled and reversible immobilization of the gamma-CA to a functionalized surface
additional information
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
additional information
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
additional information
-
immobilization of purified CA and whole cell on different biopolymer matrices, overview
additional information
-
immobilization of purified CA and whole cell on different biopolymer matrices, overview
-
additional information
-
immobilization of purified CA and whole cell on different biopolymer matrices, overview. The highest enzyme immobilization of 75% is achieved on chitosan-NH4OH beads with maximum increase of 1.08-1.18 fold stability between 35°C and 55°C
additional information
generation of Car3-knockout mice. Loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress
additional information
-
generation of Car3-knockout mice. Loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress
additional information
Mus musculus 129SEVE
-
generation of Car3-knockout mice. Loss of CAIII in soleus and tibialanterior (TA) muscles in Car3-KO mice does not change muscle mass, sarcomere protein isoform contents, and the baseline twitch and tetanic contractility as compared with age-matched wild-type controls. Car3-KO TA muscle shows faster force reduction at the beginning but higher resistance at the end during a fatigue test, followed by slower postfatigue recovery than that of wild-type TA muscle. Superfused Car3-KO soleus muscle also have faster total force reduction during fatigue test than that of wild-type soleus. It shows less elevation of resting tension followed by a better postfatigue recovery under acidotic stress
-
additional information
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
additional information
Persephonella marina DSM 14350 / EX-H1
-
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
additional information
cloning of the full domain of carbonic anhydrase from Plasmodium falciparum, which incorporates 358 amino acid residues, from 181 to 538, in the sequence of this 600 amino acid long protein, called PfCAdom. PfCAdom is 13.3times more effective as a catalyst compared to the truncated form PfCA1. One of the highly conserved zinc coordinating histidines (His119 in hCA II) is not present in the truncated enzyme form PfCA1 since a Gln residue is found in the same, a tyrosine residue instead of a histidine is present in position 64
additional information
-
cloning of the full domain of carbonic anhydrase from Plasmodium falciparum, which incorporates 358 amino acid residues, from 181 to 538, in the sequence of this 600 amino acid long protein, called PfCAdom. PfCAdom is 13.3times more effective as a catalyst compared to the truncated form PfCA1. One of the highly conserved zinc coordinating histidines (His119 in hCA II) is not present in the truncated enzyme form PfCA1 since a Gln residue is found in the same, a tyrosine residue instead of a histidine is present in position 64
additional information
generation of truncated mutant PfCA1 comprising 231 amino acids, the mutant shows 2.7fold lower kcat and a 13fold lower catalytic efficiency than enzyme PfCAdom
additional information
-
generation of truncated mutant PfCA1 comprising 231 amino acids, the mutant shows 2.7fold lower kcat and a 13fold lower catalytic efficiency than enzyme PfCAdom
additional information
-
immobilization of purified CA and whole cell on different biopolymer matrices, overview. The highest enzyme immobilization of 89% is achieved on chitosan-KOH beads
additional information
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview. Immobilizing the enzyme within solid supports improves the method. Formation of gamma-CA nanoassemblies, where individual enzymes are connected to each other and make multiple linked interactions with the reactor surface. This can be achieved by mutating specific enzyme residues to cysteines, in order to introduce sites for biotinylation, thus allowing the subsequent formation of stable nanostructures by cross-linking of biotinylated-gamma-CAs with streptavidin tetramers. Further addition of an immobilization sequence at amino- or carboxy-terminus also allows for a controlled and reversible immobilization of the gamma-CA to a functionalized surface
additional information
the truncated Nce103 without the sequence coding for the N-terminal 13 residues Nce103DELTAN13 shows almost the same activity as the full length Nce103, whereas the activity of the truncated Nce103 without the sequence coding for the N-terminal 50 residues Nce103DELTAN50 is completely abolished
additional information
-
the truncated Nce103 without the sequence coding for the N-terminal 13 residues Nce103DELTAN13 shows almost the same activity as the full length Nce103, whereas the activity of the truncated Nce103 without the sequence coding for the N-terminal 50 residues Nce103DELTAN50 is completely abolished
additional information
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
additional information
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
additional information
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
additional information
Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1
-
capture of CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
Halalkalibacterium halodurans
purified recombinant enzyme, stable for 2 h, complete loss of activity after 12 h
747660
10
4 - 13
-
activity is completely lost at a moderately acidic pH of 4.0 and a highly basic pH of 13.0
702804
5
purified recombinant enzyme mASCA, about 70% activity remaining after 15 min
747292
5 - 10
-
the enzyme retains 100% activity at pH 8.0 while more than 80% enzyme activity is retained in the pH range 7.0-8.5 after 24 h incubation at room temperature, 45% and 65% enzyme activity at pH 5.0 and 10.0 respectively
706571
5 - 8
-
stable for about 1 week, in presence of dithiothreitol or mercaptoethanol
33562
6 - 11
7 - 9
-
the enzyme retains 88% residual activity at pH 8.0, 72% residual activity at pH 8.5, and 66% residual activity at pH 9.0 following 6 h of incubation, stable at 80% of maximal activity in the pH range pH 7.0-9.0 following 3 h of incubation, effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview
715948
7.6 - 10
-
enzyme shows high stable activity at the two ranges which are around pH 7.6 and pH 10
728989
8.5
additional information
10
purified recombinant enzyme mASCA, over 90% activity remaining after 48 h, 70% after 72 h
747292
4
purified recombinant enzyme mASCA, about 30% activity remaining after 15 min
747292
6 - 11
purified recombinant enzyme mASCA, over 90% activity remaining after 15 min within this range
747292
6 - 11
Halalkalibacterium halodurans
purified recombinant enzyme, 100% activity remaining after 48 h
747660
6 - 11
Halalkalibacterium halodurans
purified recombinant enzyme, completely stable within this range for 48 h
747955
8.5
-
purified native enzyme, optimally stable, 93% of maximum activity remaining after 14 days in 10 mM Tris-HCl buffer, pH 8.5
714853
additional information
-
42%, 39% and 36% stability is observed at pH 8.0, pH 8.5, and pH 9.0, respectively for commercial bovine carbonic anhydrase following 6 h of incubation. After 3 h incubation at pH 7.0 and pH 7.5, bovin retains 81% and 75% residual activity, while 79%, 69%, 61%, stability is observed at pH 8.0, pH 8.5, and pH 9.0, respectively. Effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview
715948
additional information
-
the enzyme shows 78% stability along with 71% and 73% residual activity at pH 8.0 and pH 9.0, respectively, following 6 h of incubation, after 3 h of incubation 80% stability is observed between pH 7.5-9.0, effect of pH and temperature as function of time on stability of CAs from different species, overview
715948
additional information
-
effect of pH and temperature as function of time on stability of CAs from different species, overview
715948
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
30
30 - 100
purified recombinant His-tagged enzyme lacking the signal peptide, pH 7.6, 15 min, slow decrease in the enzyme activity at temperatures up to 50°C and almost no effect beyond 50°C up to 100°C. The enzyme retains over 80% of its activity between 60°C and 100°C, the Tm is 84.5°C
35 - 45
35 - 55
-
stable at 35-45°C, there is a progressive decline in the stability of enzyme following increase in temperature from 35°C to 55°C, the enzyme retains 100% activity at 35°C while 89% and 86% activity is retained at 40°C and 45°C respectively. In contrast, 21.0% residual activity is observed at 55°C following 1 h incubation at the respective temperatures
40
40 - 60
50
50 - 72
Halalkalibacterium halodurans
Tm of BhCA is 72°C, T1/2 values at 50°C and 60°C are 66 min and 24 min, respectively
50 - 80
Halalkalibacterium halodurans
the T1/2 values at 50°C, 60°C, 70°C, and 80 °C are 72, 32, 7.0, and 2.0 min
55 - 60
the melting temperature is around 55°C without the addition of ligand, and shifts to 60°C or higher when the added ligand binds and stabilizes the protein
55 - 75
-
the purified enzyme retains catalytic activity if incubated for 15 min at 55°C, but only a little activity is recovered when the enzyme is incubated above 75°C
60
65
purified recombinant enzyme mASCA, retains over 90% activity after 15 min
70
71.9
the enzyme has a melting temperature of 71.9°C at pH 8.0. TcruCA presents two transition peaks: one between 58°C and 62°C and the other between 68°C and 72°C, dependent on the pH
75
75 - 90
enzyme Cab retains its activity after incubation at temperatures up to 75°C for 15 min, whereas poor activity is recovered when the enzyme is incubated at temperatures of 90°C or higher
80
purified recombinant His-tagged enzyme, pH 8.3, 40% activity remaining after 30 min, complete inactivation after 60 min
85
most thermostable carbonic anhydrase, retains 90% activity after incubation for 15 min
additional information
100
-
purified enzyme SazCA is able to retain CO2 hydration activity after incubation for 3 h
30
-
the enzyme possesses two stable folded conformers with the conformational transition occurring at about 30°C. The methodology yields a stability curve for the complete unfolding of the enzyme below this temperature but only the partial unfolding, to the molten globule state, above it. The transition state thermodynamics for the low-term to physiological-temperature conformational change are calculated from slow-scan-rate differential scanning calorimetry measurements where it is found that the free energy barrier for the conversion is 90 kJ/mole and the transition state possesses a substantial unfolding quality
40 - 60
thermal unfolding of recombinant isotope-labeled isozyme at different pH values of pH 5.5-8.5, overview
40 - 60
thermal unfolding of recombinant isotope-labeled isozyme at different pH values of pH 5.5-8.5, overview. The protein appears to be more temperature stable at pH 7.5-8.5 compared to pH 5.5
70
-
at the pasteurization temperature of 70°C, the enzyme activity of carbonic anhydrase is 100% after 1 h, 97% after 2 h, and 94% after 3 h, freeze-dried enzyme. For the enzyme in solution, 87.6% activity remains after 30 min, 81.5% after 1 h, 62% after 2 h, and 50% activity remains after 3 h
additional information
-
effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview
additional information
Halalkalibacterium halodurans
the thermal unfolding of recombinant BhCA is studied by using circular dichroism
additional information
thermal stability and thermal unfolding analyses of wild-type enzyme and mutants M1-M4, overview
additional information
-
effect of pH and temperature as function of time on stability of carbonic anhydrases from different species, overview
additional information
-
the enzyme exhibits more than 80% stability between pH 7.0 and pH 8.0, while 68% and 57% are retained at pH 8.5 and pH 9.0 after 3 h of incubation. The enzyme retains 63%, 54% and 45% residual activity at pH 8.0, pH 8.5, and pH 9.0, respectively, following 6 h of incubation. Effect of pH and temperature as function of time on stability of CAs from different species, overview
additional information
-
effect of pH and temperature as function of time on stability of CAs from different species, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
a key role for sodium ions in increasing halotolerant enzyme stability largely through interactions with the highly ordered first Na+ hydration shell, molecular dynamics calculations, overview
dialysis against pyridine dicarboxylate, at 15°C, 98% loss of activity after 24 h
Macropus eugenii desmarest
-
enzyme appears to denature with a midpoint of a structural transition near 2.1 M denaturant guanidine hydrochloride
-
enzyme retains conformational stability in low and high salt concentrations
-
freezing and thawing results in formation of aggregates, unfolded at 1.5 M guanidine hydrochloride
presence of salt, 0-4 M NaCl, during Dca storage has no effect on the enzyme stability and activity
the enzymes polyhemoglobin, superoxide dismutase, catalase, and carbonic anhydrase (SFHb, SOD, CAT, CA) are all cross-linked together to form a nano-sized soluble blood substitute. The enzymes activities of the freeze-dried cross-linked enzyme complex poly-[SFHb-SOD-CAT-CA] are more stable compared with the soluble poly-[SFHb-SOD-CAT-CA] and even more so when compared to the uncrosslinked solution of free SFHb, SOD, CAT and CA enzymes
-
the purified protein is unstable in the absence of glycerol and aggregates irreversibly
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme loses activity when it is exposed to air or 3% H2O2
727748
the enzyme produced in vivo is sensitive to oxygen, losing 90% of activity in 5 min after exposure to air
-
696355
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-14°C, enzyme as a suspension in saturated (NH4)2SO4 containing 0.02 M sodium phosphate buffer, 0.1 M NaCl and 0.001 M EDTA, pH 6.8, stable for 2 months
-
-20°C, Tris-SO4, pH 8.8, purified enzyme, solution remains fully soluble and active for at least 2 months
-80°C, recombinant bacterial cell pellets can be stored for several months without apparent loss in enzyme activity
0°C, activity remains stable during the first months in storage but gradually declines to 25% of the initial value after 1 year storage
-
4°C, Tris-SO4, pH 8.8, purified enzyme, solution remains fully soluble and active for at least 2 months
after 40 days storage, the free hCA I sustains 50% and 0.11% of its original activity, whereas the immobilized hCA I retains 89% and 85% of its original activity at 4°C and 25°C, respectively
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
ammonium sulfate fractionation and 4-aminomethylbenzenesulfonamide agarose column chromatography
-
glutathione Sepharose 4B column chromatography and sulfonamide affinity chromatography
-
GSTrap resin chromatography and NHS-activated Sepharose 4 Fast Flow resin chromatography
-
improved method for the purification of the carbonic anhydrase isozymes by affinity chromatography
-
isozyme CA II, recombinant wild-type isozyme CA II and chimeric CA IX mimic mutant isozyme from Escherichia coli strain BL21(DE3) by p-aminomethylbenzenesulfonamide affinity chromatography
isozyme CA IX, recombinant wild-type isozyme from Escherichia coli strain BL21(DE3) by p-aminomethylbenzenesulfonamide affinity chromatography
mutant enzyme N67L is purified by affinity chromatography using 4-(aminomethyl)benzenesulfonamide coupled to agarose beads
native enzyme 303.9fold from gills by L-tyrosine-sulfanilamide affinity chromatography
-
native enzyme 349fold by L-tyrosine-sulfanilamide affinity chromatography
Salmo trutta Labrax Coruhensis
-
native enzyme 35fold from spermatheca by L-tyrosine-sulfanylamide affinity chromatography, elution with 1 M NaCl/25 mM Na2HPO4, pH 6.3
-
native enzyme 539fold by one-step affinity chromatography on L-tyrosine sulphonamide
-
native enzyme 78.8fold from liver by single step tyrosine sulfanilamide affinity chromatography
-
native enzyme 91fold by L-tyrosine-sulfanilamide affinity chromatography, elution with 1 M NaCl/25 mM Na2HPO4, pH 6.3
-
native enzyme by anion exchange and hydrophobic interaction chromatography, followed by gel filtration
-
native enzynme from erythrocytes, 203fold by L-tyrosine sulfanilamide affinity chromatography
-
native enzynme from erythrocytes, 243fold by L-tyrosine sulfanilamide affinity chromatography, to homogeneity
-
native hCA I and hCA II from erythrocytes by aniline-sulfanylamide affinity chromatography
-
native isozyme hCA I from erythrocytes isolated from human blood by cellulose-benzyl-sulfanilamide affinity chromatography, elution with 1 M NaCl/25 mM Na2HPO4, pH 6.3
native isozyme hCA I from human blood erythrocytes by L-tyrosine-p-aminobenzene sulfonamide affinity chromatography
native isozyme hCA I from human blood erythrocytes by L-tyrosine-sulfanilamide affinity chromatography and elution with 1.0 M NaCl/25 mM Na2HPO4, pH 6.3
native isozyme hCA II from erythrocytes isolated from human blood by cellulose-benzyl-sulfanilamide affinity chromatography, elution with 0.1 M CH3COONa/0.5 M NaClO4, pH 5.6
native isozyme hCA II from human blood erythrocytes by L-tyrosine-sulfanilamide affinity chromatography and elution with 0.1 M NaCH3COO/0.5 M NaClO4, pH 5.6
native soluble enzyme from mantle by ammonium sulfate fractionation, anion exchange chromatography, and pAMBS affinity chromatography, to homogeneity
Ni2+ affinity column chromatography and Superdex 75 gel filtration
recombinant
recombinant enzyme
recombinant enzyme from Escherichia coli anaerobically or aerobically, recombinant enzyme from Methanosarcina acetivorans anaerobically
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by 4-aminomethylbenzenesulfonamide agarose affinity chromatography and ultrafiltration
recombinant enzyme from Escherichia coli strain BL21(DE3) by p-(aminomethyl)-benzenesulfonamide affinity chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) by p-amino-methyl-benzenesulfonamide affinity chromatography and gel filtration, followed by ultrafiltration
recombinant enzymes
recombinant extracellular enzyme from Pichia pastoris strain GS115 culture supernatant by ultrafiltration, acetone precipitation, and pAMBS affinity chromatography
Halalkalibacterium halodurans
recombinant GST-tagged isozyme hCA IX from Escherichia coli strain BL21 Codon Plus by glutathione affinity chromatography and sulfonamide affinity chromatography
recombinant His-tagged bsCA II from Escherichia coli by cobalt affinityy chromatography
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatagraphy
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and gel filtration, followed by pAMBS affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) medium by nickel affinity chromatography
Halalkalibacterium halodurans
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)/ArcticExpress DE3 cells by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by cobalt affinity chromatography and dialysis
recombinant His-tagged isozyme CA XIV from Escherichia coli strains to 96% purity by nickel affinity chromatography, dialysis, and 4-aminomethylbenzenesulfonamide affinity chromatography (elution by a linear gradient of 0.5 M sodium perchlorate using 0.1 M sodium acetate and 0-0.5 M sodium perchlorate, pH 5.6)
recombinant His-tagged isozyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged isozyme HCAII by nickel affinity chromatography, ultrafiltration, and gel filtration, to homogeneity
recombinant His-tagged PG domain of isozyme CA9 IX from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by protease enzyme SenP2, and another step of nickel affinity chromatography to remove the tag
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and dialysis
recombinant is-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3)pLysS by nickel affinity chromatography, gel filtration, and tag cleavage by TEV protease, followed by dialysis, another step of nickel affinity chromatography, anion exchange chromatography, gel filtration, and ultrafiltration
recombinant isozymes CAH-3, CAH-4a and CAH-5 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant mutants V47A and G41A to homogeneity from Escherichia coli by ion exchange and hydrophobic interaction chromatography, and gel filtration
recombinant soluble His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography from the supernatant, and recombinant renatured His-tagged enzyme from inclusion bodies by nickel affinity chromatography, both enzyme forms are active
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by affinity chromatography on a 4-(aminomethyl)-benzene-sulfonamide resin
-
Sephadex G-75 gel filtration, DEAE cellulose column chromatography, and Sepharose-4B-L tyrosine sulfanilamide column chromatography
-
Sepharose-IDA-Ni+2 column chromatography, S-Sepharose column chromatography, gel filtration
Super Q Toyopearl 650M column chromatography, Resource Q column chromatography, Bio-Scale CHT-20-I column chromatography, and Superdex 200pg gel filtration
the enzyme from a commercial preparation is further purified by gel filtration and ultrafiltration
-
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Synechocystis sp. PCC 6803 / Kazusa
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)/ArcticExpress DE3 cells by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)/ArcticExpress DE3 cells by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
alpha-carbonic anhydrase gene cloned and sequenced, truncated gene expressed in Escherichia coli BL21(DE3)
-
Arabidopsis thaliana plant transformation for expression of mutant enzymes via Agrobacterium tumefaciens strain GV3101
beta class isozymes bsCA I and bsCA II, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged bsCA II in Escherichia coli
BhCA, recombinant constitutive extracellular expression of the enzyme in Pichia pastoris strain GS115 under methanol inducible (AOX1) as well as constitutive (GAP) promoters, the recombinant enzyme is secreted. The double transformant of the strain GS115 harboring BhCA under both AOX1 and GAP promoters possessed two copies of the gene
Halalkalibacterium halodurans
CA I and CA II cDNA expressed in Escherichia coli BL21 (DE3)
CA I and CA II cDNA expressed in Escherichia coli BL21 (DE3), cDNA hCA IX PCR amplified
-
CA I and CA II cDNAs expressed in Escherichia coli BL21 (DE3)
cDNA cloned and expressed in Saccharomyces cerevisiae, also expressed in Escherichia coli
cloned and overexpressed
cloning of isozyme CA XIII, phylogenetic analysis, quantitative real-time PCR expression analysis
-
cloning of the full domain of carbonic anhydrase from Plasmodium falciparum, which incorporates 358 amino acid residues, from 181 to 538, in the sequence of this 600 amino acid long protein, called PfCAdom
coexpressed in tsA201 cells expressing heterologous fluorescent fusion proteins CAII-CyPet and YPet-AE1
-
DNA and amino acid sequence determination and analysis of PgiCAb, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree
enzyme form PfCAdom comprising 358 amino acids (residue 181 to residue 538), recombinant expression of His-tagged enzyme PfCAdom
expressed as a His-tagged fusion protein in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli and in a baculovirus-Sf9 insect cell expression system, the recombinant proteins consist of either the CA IX catalytic domain only or the extracellular domain, which includes both the proteoglycan and catalytic domains, lacking the small transmembrane and intracytoplasmic regions of CA IX
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells using the baculovirus-insect cell expression system
expressed in Escherichia coli BL21(DE3)pLysS cells
expression in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
-
gene Ca, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, comparative real-time quantitative PCR, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene ca1, encoding delta-CA, sequence comparisons, phylogenetic analysis, recombinant His-tagged enzyme expression in Escherichia coli
gene CA14, recombinant expression in Escherichia coli: effect of different promoters, Escherichia coli strains (Rosetta 2(DE3), Rosetta-gami 2 (DE3), Origami B (DE3), and BL21 trxB (DE3)), and the length of recombinant CA XIV protein construct are analyzed for the production CA XIV in large scale by using affinity purification, method evaluation and optimization, overview. The most suitable Escherichia coli strain is Origami B (DE3)
gene CA2, cloned from DNA of outer and inner mantle, DNA and amino acid sequence determination and analysis, no nucleotide polymorphism is observed between the CA2-like cDNA sequences obtained from these two tissues, phylogenetic analysis, quantitative real-time PCR expression analysis of CA2-like
gene CA2, recombinant expression in Escherichia coli strain BL21(DE3), optimization of expression media and cell culture conditions to produce high levels of 3 different deuterated human carbonic anhydrases (hCAs). The labeled hCAs are then characterized and tested for deuterium incorporation by mass spectrometry, temperature stability, and propensity to crystallize, overview
gene CA2, recombinant expression of the enzyme in Escherichia coli strain BL21(DE3)
gene CA2, recombinant expression of wild-type and mutant enzymes in Escherichia coli
gene CA3, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative RT-PCR expression analysis
gene CA5A, localized to chromosome 16q24.3, an unprocessed pseudogene is assigned to 16p12, recombinant His-tagged enzyme expression in Escherichia coli strain BL21(DE3) from plasmid pENTR223 as soluble enzyme and in inclusion bodies
gene ca6, isolation and sequencing of Danio rerio CA VI cDNA, complete with the sequence coding for the PTX domain, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression of the recombinant CA VI-PTX protein in Spodoptera frugiperda Sf9 cells using the baculovirus expression system, quantitative real-time PCR
gene CA9, recombinant expression in Escherichia coli strain BL21(DE3), optimization of expression media and cell culture conditions to produce high levels of 3 different deuterated human carbonic anhydrases (hCAs). The labeled hCAs are then characterized and tested for deuterium incorporation by mass spectrometry, temperature stability, and propensity to crystallize, overview. Deuteration highly reduces the enzyme yield
gene can, sequence comparisons and phylogenetic analysis, recombinant overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
gene ccmM, CcmM sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene CpsCAgamma, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) (Arctic Express DE3 competent cells), subcloning in Escherichia coli strain DH5alpha
gene DmBCA, phylogenetic analysis, expression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
gene icfA, CcaA sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Synechocystis sp. PCC 6803 / Kazusa
gene PERMA_1443, phylogenetic tree, recombinant expression of His-tagged enzyme lacking the signal peptide from codon-optimized carbonic anhydrase gene in Escherichia coli strain BL21(DE3), real-time PCR enzyme expression analysis
gene PhaCAgamma, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)(ArcticExpress DE3 competent cells), subcloning in Escherichia coli strain DH5alpha
gene Tcr_1545, sequence comparisons, recombinant enzyme expression in Escherichia coli strain BL21(DE3)
genes cah-1, cah-2, cah-3, cah-4, cah-5, and cah-6, real-time RT-PCR expression analysis, overview. Gene cah-3 is able to complement the function of Saccharomyces cerevisiae CA, NCE103, in vivo, expression in Saccharomyces cerevisiae wild-type strain CEN.PK2 and in mutant strain CEN.HE28-1A. Recombinant expression of His-tagged CAH-3, CAH-4a and CAH-5 in Escherichia coli strain BL21(DE3), but in vitro activity is only detectable for CAH-4a
-
isozyme CA II, recombinant expression of wild-type isozyme CA II and chimeric CA IX mimic mutant isozyme in Escherichia coli strain BL21(DE3)
isozyme CA IX, recombinant expression of wild-type isozyme in Escherichia coli strain BL21(DE3)
isozyme carbonic anhydrase 6, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, quantitative real-time PCR and quantitative/semiquantitative RT-PCR expression analysis
A0A2D1CFJ9
isozyme hCAII, expression in Escherichia coli strain BL21(DE3) from the plasmids pET-28b/hCA II
-
isozyme LjCAA1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis by quantitative real-time RT-PCR, and spatial expression profiling, recombinant expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)
isozyme LjCAA2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression analysis by quantitative real-time RT-PCR, and spatial expression profiling, recombinant expression of His-tagged isozymes in Escherichia coli strain BL21(DE3)
overexpressed in Escherichia coli
overexpressed in transformed Escherichia coli cultures, expression in yeast, complements the growth defect in a yeast beta-CA knockout in Saccharomyces cerevisiae DELTA NCE103
overexpression in Escherichia coli
overexpression of HICA in Escherichia coli in minimal media supplemented with CoCl2
-
overexpression of wild-type enzyme and mutants V47A and G41A in Escherichia coli
recombinant enzyme expression in Escherichia coli or in Methanosarcina acetivorans
-
recombinant expression of GST-tagged isozyme hCA IX in Escherichia coli strain BL21 Codon Plus
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged PG domain of isozyme CA9 IX in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)pLysS
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) achieving a 31.4fold enhancement in CA production for the wild-type, subcloning in Escherichia coli strain DH5alpha. About 50% of wild-type enzyme produced is secreted when recombinant Escherichia coli harboring BhCA-pET22b is cultivated in a medium with EDTA and lysozyme because of the efficient pelB leader sequence, cultvation parameters are optimized for rBhCA secretion
Halalkalibacterium halodurans
recombinant expression of soluble His-tagged enzyme in Escherichia coli strain ArcticExpress (DE3)RIL
recombinant overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
using the baculovirus expression system as a His-tagged fusion protein
wild-type and variant carbonic anhydrases heterologously produced in Escherichia coli BL21(DE3)
-
wild-type and variants expressed in Escherichia coli BL21(DE3) or BL21(DE3) Gold
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CAIX expression is 5-7fold induced by hypoxia and is significantly associated with tumor grade and poor survival, overview
-
carbonic anhydrase activity shows week sensitivity to in vitro cadmium exposure, while it is significantly increased (about 40%) following two weeks in vivo exposure (0.001785 mM cadmium), additionally protein expression appears significantly enhanced. When exposed for 30 days to the cadmium-polluted site of Mar Grande of Taranto mussels show a very significant increase in the carbonic anhydrase activity (about 26% increase)
-
exposure to light induces significant increases in the protein abundance of CA2-like in the outer mantle
expression of CA IX is strongly increased in many types of tumors, such as gliomas/ependymomas, mesotheliomas, and papillary/follicular carcinomas, as well as carcinomas of the bladder, uterine cervix, kidneys, esophagus, lungs, head and neck, breast, brain, vulva, and squamous/basal cell carcinomas
-
feeding stress is used to upregulate CO2 excretion pathways: significant upregulation of isozyme CA II is observed, while isozyme CA XIII is strongly downregulated
-
gene expression is induced by increased medium pH
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
the gene encoding isozyme LjCAA1 is slightly to moderately down-regulated in ineffective nodules formed by mutant Mesorhizobium loti strains
the gene encoding isozyme LjCAA2 is slightly to moderately down-regulated in ineffective nodules formed by mutant Mesorhizobium loti strains
the transcript and protein levels of DDCA/DDCA in the ctenidium of Tridacna squamosa increase significantly after 6 and 12 h of exposure to light, respectively
transcript levels of specific CA subunits depend on the CO2 level in air
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
the expression of the gene encoding CamH is substantially greater in acetate-grown cells than in methanol- or trimethylamine-grown cells
-
-
the gene encoding isozyme LjCAA1 is slightly to moderately down-regulated in ineffective nodules formed by mutant Mesorhizobium loti strains
the gene encoding isozyme LjCAA1 is slightly to moderately down-regulated in ineffective nodules formed by mutant Mesorhizobium loti strains
-
-
the gene encoding isozyme LjCAA2 is slightly to moderately down-regulated in ineffective nodules formed by mutant Mesorhizobium loti strains
the gene encoding isozyme LjCAA2 is slightly to moderately down-regulated in ineffective nodules formed by mutant Mesorhizobium loti strains
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli inclusion bodies by solubilization of the purified inclusion bodies in 50 mM phosphate buffer, pH 7.0, 300 mM NaCl, and 1% N-lauroylsarcosine, and incubation on rocker for 30 min, or by dialyzing the solution against 50 mM phosphate buffer, pH 7.0, and 150 mM NaCl for 24 h at 4°C, and then followed by centrifugation of the solubilized inclusion bodies for 30 min at 12000 rpm
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
-
activity of carbonic anhydrase is significantly lower in patients with renal cell carcinoma than in controls. The marker carbonic anhydrase might be potentially important as an additional biochemical tool for diagnosing renal cell carcinoma
drug development
environmental protection
medicine
additional information
analysis
-
carbonic anhydrase assay based on membrane inlet mass spectrometry. A quantitative assessment of the carbonic anhydrase activity in photosystem II
analysis
-
carbonic anhydrase may serve as a biochemical marker for photosynthetic capacity in teak genotypes
drug development
-
Drosophila beta-CA represents a highly active mitochondrial enzyme that is a potential model enzyme for anti-parasitic drug development
drug development
discovery and development of carbonic anhydrase inhibitors is crucial for their clinical use as antiepileptic, diurectic, and antiglaucoma agents
drug development
superfamily of metalloenzymes carbonic anhydrases (CAs) has a potential as druggable enzymes to limit the development of Plasmodium falciparum gametocytes
drug development
the isozymes CA IVX is a possible drug target for the treatment of epilepsy, some retinopathies, and skin tumors
environmental protection
-
the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst
environmental protection
-
the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst
environmental protection
-
the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst
environmental protection
-
the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst
environmental protection
Caminibacter sp.
-
carbon dioxide absorption into carbonate solutions, promoted by the enzyme carbonic anhydrase, is proposed as potential technology for CO2 capture. The use of solid CA-based biocat-alysts allows the enzyme recovery and reuse under continuous operating conditions typical of industrial applications
environmental protection
recombinant engineered mASCA enzyme exhibits high production yield and sufficient stabilities against relatively high temperature and alkaline pH, which are required conditions for the development of more efficient enzymatic CCS systems. Carbon capture and storage (CCS) is a technology that can capture up to 90% of the carbon dioxide (CO2) emissions produced from the use of fossil fuels in electricity generation and industrial processes, preventing the carbon dioxide from entering the atmosphere. mASCA has the potential to play an important role in CCS systems, particularly in an enzyme-based CO2 capture system that requires large amounts of CA enzyme
environmental protection
-
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
-
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
environmental protection
-
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
environmental protection
-
the enzyme can be useful in biomimetic sequestration of CO2 into CaCO3 as a biological catalyst
-
environmental protection
Desulfovibrio vulgaris Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303
-
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
environmental protection
Persephonella marina DSM 14350 / EX-H1
-
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
environmental protection
Methanothermobacter thermautotrophicus ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg
-
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
environmental protection
Thermovibrio ammonificans DSM 15698 / JCM 12110 / HB-1
-
the enzyme is useful to capture CO2 from flue gas in bio-mimetic CO2 capture systems to reduce the concentration of CO2 in the atmosphere, method technology, overview
-
medicine
-
design of novel antitumor properties, mainly for hypoxic tumors that overexpress CA IX
medicine
-
overexpressed on cell surfaces of certain cancers, potential target for chemotherapeutic agents
medicine
relevance for the drug design of novel CA inhibitors, intersting pharmacological applications
medicine
-
there are amino acid differences in the active site of AaCA1 of Aedes aegypti and human carbonic anhydrases. Terefore this enzyme could be a potential drug target of selective carbonic anhydrase inhibitors for the control of mosquito populations and the pathogens they carry
medicine
CA IX is a marker of tumor hypoxia and a prognostic factor in several human cancers, inhibition of this enzyme shows antitumor activity both in vitro and in vivo
medicine
-
isoform CA IX is used as a marker of tumor hypoxia and as a prognostic factor for many human cancers
medicine
-
isozyme CAIX is a marker for hypoxic tumors and is correlated with poor prognosis in breast cancer patients
additional information
Halalkalibacterium halodurans
carbonic anhydrase is a biocatalyst that catalyzes the hydration of CO2 to bicarbonate and protons, thus useful in mitigating green house effect by sequestering CO2 from various point sources
additional information
immobilized hCA I on the magnetic nanoparticles has high operational stability and magnetic recovery which is desirable for biotechnological applications
additional information
Halalkalibacterium halodurans TSLV1
-
carbonic anhydrase is a biocatalyst that catalyzes the hydration of CO2 to bicarbonate and protons, thus useful in mitigating green house effect by sequestering CO2 from various point sources
-
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 4.2.1.1)
Transporter Classification Database (TCDB): 8.A.164.1.1, 2.A.53.3.12
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Release 2023.1 (January 2023)
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