Information on EC 3.4.17.1 - carboxypeptidase A

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.4.17.1
-
RECOMMENDED NAME
GeneOntology No.
carboxypeptidase A
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
mechanism
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
relationships between structure and mechanism, zinc environment and substrate complexes
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
mechanisms elucidated from complex with inactivator 2-benzyl-3-iodo-propanoic acid
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
pK values of active site residues, analysis of kinetics and mechanism under alkaline conditions
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
molecular dynamics characterization of active cavity
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
conceptual model of relationship between activity, mechanism and conformational mobility
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
rapid release: Tyr, Phe, Trp, Leu, Ile, Thr, Gln, His, Ala, Val, homoserine, slow release: Asn, Ser, Lys, MetSO2, very slow release: Gly, Asp, Glu, CySO3H, S-carboxymethylcysteine, not released: Pro, Hyp, Arg
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
evidence of general base pathway
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
relationships between structure and mechanism, different catalytic sites for esters and peptides, role of mechanic strain discussed
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
correlations between mechanism, kinetics, and structure, intermediates and rate-determining steps
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
evidence for acyl-enzyme intermediates
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
relationships between enzyme structure and catalytic properties, catalytic groups, intermediates, and conformational changes during catalysis conform to "induced fit hypothesis"
-
-
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
cryospectrokinetic characterization of intermediates, time-course of reaction
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
promoted water pathway, mechanistic model
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
catalytic mechanism involving the Zn2+ ion and residue Glu270 with ester or protein substrates, the tetrahydrate transition state is stabilized by Arg127, overview
-
release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
show the reaction diagram
residues Glu270 and Arg127 are important for activity, the catalytic triad consists of Ile275, Tyr248, and Ala250, residues at positions 202, 254, and 268 are important for substrate specificity
Q8AXN4
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
-
-
hydrolysis
-
-
hydrolysis
Phaffia rhodozyma CBS 5905
-
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
exopeptidase, cleaves from C-terminus
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A-type metallocarboxypeptidase
-
-
Anson's enzyme
-
formerly
ASPA
-
-
aspartoacyclase
-
-
carboxypeptidase
-
-
carboxypeptidase
Phaffia rhodozyma CBS 5905
-
-
-
carboxypeptidase a
-
-
carboxypeptidase a
P00730
-
carboxypeptidase a
Cephalopina titillator
-
-
carboxypeptidase a
-
-
carboxypeptidase a
P00731
-
carboxypeptidase a
-
-
carboxypeptidase a
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
-
carboxypeptidase A-6
Q5U901
-
carboxypeptidase A-like activity
-
-
carboxypeptidase A1
Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
-
carboxypeptidase A1
-
-
carboxypeptidase A2
Q0QWG2
-
Carboxypeptidase A3
-
-
-
-
Carboxypeptidase A3
-
-
Carboxypeptidase A3
P15088
-
carboxypeptidase A4
-
-
carboxypeptidase vitellogenic-like
-
-
carboxypeptidase-A
-
-
carboxypolypeptidase
-
-
-
-
colon mast cell carboxypeptidase
-
-
CPA
P00730
-
CPA
-
-
CPA
-
-
CPA1
-
-
CPA3
-
-
CPA3
P15088
-
CPA3
-
-
CPA4
-
-
CPA4
-
CPA4 is originally referred to as CPA3 but is renamed CPA4 to reflect the order in which the CPAs are discovered
CPA6
Q5U901
-
CPAI
-
-
CPD
-
-
EC 3.4.12.2
-
-
formerly
-
EC 3.4.2.1
-
-
formerly
-
hCPA4
-
-
mast cell carboxypeptidase A
P15088
-
mast cell carboxypeptidase A
-
-
mast cell CPA
-
-
mast cell-CPA
-
-
mast-cell carboxypeptidase A
-
-
mast-cell CPA
-
-
MC-CP
-
-
MC-CPA
-
-
-
-
MC-CPA
P15088
-
MC-CPA
-
-
MC-CPA
-
-
MC-CPA
-
; mast cell carboxypeptidase A
MCP-2
Q6ZXB9
-
MDCP-A1
Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
-
MDCP-A2
Q0QWG2
-
MF-CPA
-
-
MF-CPA
Q60F93
-
molting carboxypeptidase A
-
-
molting fluid carboxypeptidase A
-
-
Nna1/CCP1
Mus musculus C57B6
-
-
-
ochratoxin A hydrolytic enzyme
-
-
PTD012
-
-
RMC-CP
-
-
-
-
vitellogenic-like carboxypeptidase
-
-
molting fluid carboxypeptidase A
Q60F93
-
additional information
-
the enzyme belongs to the metallocarboxypeptidase
CAS REGISTRY NUMBER
COMMENTARY
11075-17-5
-
9031-98-5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MF-CPA
SwissProt
Manually annotated by BRENDA team
also two allotypic forms known; overview, forms alpha, beta, gamma, and delta may result from slightly different activation conditions
-
-
Manually annotated by BRENDA team
heterogeneity: 5 molecular species that differ in amino acid composition and heat stability, but not in catalytic properties
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
overview, forms alpha, beta, gamma, and delta may result from slightly different activation conditions
-
-
Manually annotated by BRENDA team
several isoenzymes that differ in amino acid composition
-
-
Manually annotated by BRENDA team
Cephalopina titillator
-
-
-
Manually annotated by BRENDA team
banana weevil
-
-
Manually annotated by BRENDA team
cotton bollworm
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
C57B6 mice
-
-
Manually annotated by BRENDA team
cathepsin B or E deficient mice strains backcrossed into C57BL/6 mice
-
-
Manually annotated by BRENDA team
CPA6 precursor
SwissProt
Manually annotated by BRENDA team
young male and female BALB/c mice
-
-
Manually annotated by BRENDA team
Mus musculus C57B6
C57B6 mice
-
-
Manually annotated by BRENDA team
preprocarboxypeptidase A1; Japanese flounder, female
SwissProt
Manually annotated by BRENDA team
2 components: I, II
-
-
Manually annotated by BRENDA team
carboxypeptidase A 2, evolutionary relationships between rat carboxypeptidases
-
-
Manually annotated by BRENDA team
carboxypeptidase A1
-
-
Manually annotated by BRENDA team
male wistar rat
-
-
Manually annotated by BRENDA team
rabbitfish
-
-
Manually annotated by BRENDA team
beta and gamma form
-
-
Manually annotated by BRENDA team
3 electrophoretically distinct forms
-
-
Manually annotated by BRENDA team
clone ID AM1-02, carboxypeptidase A
UniProt
Manually annotated by BRENDA team
clone ID AM1-30, carboxypeptidase A homolog
UniProt
Manually annotated by BRENDA team
clone ID AM1-72, carboxypeptidase A homolog
UniProt
Manually annotated by BRENDA team
clone ID AM2-51, carboxypeptidase A
UniProt
Manually annotated by BRENDA team
clone ID AM2-60, carboxypeptidase A
UniProt
Manually annotated by BRENDA team
clone ID AM3-75, carboxypeptidase A
UniProt
Manually annotated by BRENDA team
clone ID L4-60, carboxypeptidase A
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
CPA participates in the apolysis of the integument during larval molting and metamorphosis
physiological function
-
CPA4 functions in neuropeptide processing and regulation in the extracellular environment
physiological function
-
MC-CPA plays a role in regulating innate immunity responses, including the degradation of harmful substances such as the vasoconstrictive factor endothelin 1 and snake venomtoxins
physiological function
-
molting fluid carboxypeptidase A is involved in degradation of the proteins from the old cuticle and recycling of the amino acids, the enzyme plays important role in hydrolyzing the vitellogenic proteins which are the source of nutrition for maintaining embryonic development
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Ala)4 + H2O
(Ala)3 + L-Ala
show the reaction diagram
-
-
-
ir
(S)-hippuryl-alpha-MePhe + H2O
?
show the reaction diagram
-
-
-
?
(S)-hippuryl-alpha-methylphenyllactic acid + H2O
?
show the reaction diagram
-
-
-
?
(S)-hippuryl-OPhe + H2O
?
show the reaction diagram
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Ala + H2O
3-(2-furyl)acryloyl-L-Phe + L-Ala
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Ile + H2O
3-(2-furyl)acryloyl-L-Phe + L-Ile
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Leu + H2O
3-(2-furyl)acryloyl-L-Phe + L-Leu
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Met + H2O
3-(2-furyl)acryloyl-L-Phe + L-Met
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Phe + H2O
3-(2-furyl)acryloyl-L-Phe + L-Phe
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Trp + H2O
3-(2-furyl)acryloyl-L-Phe + L-Trp
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloyl-L-Phe-L-Val + H2O
3-(2-furyl)acryloyl-L-Phe + L-Val
show the reaction diagram
-
-
-
-
?
4-chlorocinnamoyl-L-beta-phenyllactate + H2O
4-chlorocinnamic acid + L-beta-phenyllactate
show the reaction diagram
-
-
-
-
?
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-L-beta-phenyllactate + H2O
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala + L-beta-phenyllactate
show the reaction diagram
-
-
-
ir
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-Phe + H2O
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala + L-Phe
show the reaction diagram
-
-
-
ir
Ac-Phe-ThiaPhe + H2O
Phe + ThiaPhe
show the reaction diagram
-
-
-
-
?
alpha-Tubulin + H2O
?
show the reaction diagram
Mus musculus, Mus musculus C57B6
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
partial cleavage of about 50% of angiotensin is found after 30 min of incubation with CPA4
-
-
?
angiotensin I + H2O
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His + Leu
show the reaction diagram
-
-
-
ir
angiotensin I + H2O
angiotensin II + His-Leu
show the reaction diagram
-
shown in an ex vivo system of peritoneal exudates cells
-
-
?
angiotensin I + H2O
des-Leu10 angiotensin I + Leu
show the reaction diagram
-
-
-
-
?
anisylazoformyl-L-Phe + H2O
anisylazoformic acid + L-Phe
show the reaction diagram
-
-
-
?
apoB-100 + H2O
?
show the reaction diagram
-
-
-
-
?
apolipoprotein B + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate + H2O
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate + ?
show the reaction diagram
-
-
-
ir
benzoyl-Gly-Gly-L-Phe + H2O
benzoyl-Gly-Gly + L-Phe
show the reaction diagram
-
-
-
ir
benzoyl-Gly-Gly-L-Phe + H2O
benzoyl-Gly-Gly + L-Phe
show the reaction diagram
-
-
-
ir
benzoyl-Gly-Gly-L-Phe + H2O
benzoyl-Gly-Gly + L-Phe
show the reaction diagram
-
-
-
ir
benzoyl-Gly-L-Phe + H2O
benzoyl-Gly + L-Phe
show the reaction diagram
-
-
-
ir
benzoyl-Gly-L-Phe + H2O
benzoyl-Gly + L-Phe
show the reaction diagram
-
-
-
ir
benzoyl-Gly-L-Phe + H2O
benzoyl-Gly + L-Phe
show the reaction diagram
-
-
-
ir
benzoyl-Gly-phenyllactate + H2O
benzoyl-Gly-phenyllactate + ?
show the reaction diagram
-
-
-
ir
Benzyloxycarbonyl-Ala-Phe + H2O
Benzyloxycarbonyl-Ala + Phe
show the reaction diagram
-
-
-
ir
Benzyloxycarbonyl-Gly-Phe + H2O
Benzyloxycarbonyl-Gly + Phe
show the reaction diagram
-
-
-
ir
benzyloxycarbonyl-Phe-Leu + H2O
benzyloxycarbonyl-Phe + Leu
show the reaction diagram
-
-
-
ir
beta-actin (169-177) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
big SAAS + H2O
?
show the reaction diagram
-
good substrate
-
-
?
carbobenzoxy-Gly-Gly-L-Tyr + H2O
carbobenzoxy-Gly-Gly + L-Tyr
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-Gly-Leu + H2O
carbobenzoxy-Gly-Gly + Leu
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-Gly-Phe + H2O
carbobenzoxy-Gly-Gly + Phe
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-Gly-Val + H2O
carbobenzoxy-Gly-Gly + Val
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Leu + H2O
carbobenzoxy-Gly + L-Leu
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Leu + H2O
carbobenzoxy-Gly + L-Leu
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Phe + H2O
carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Trp + H2O
carbobenzoxy-Gly + L-Trp
show the reaction diagram
-
-
-
ir
carbobenzoxy-Gly-L-Trp + H2O
carbobenzoxy-Gly + L-Trp
show the reaction diagram
-
-
-
ir
carbobenzyloxy-Gly-hippuryl-L-Phe + H2O
carbobenzyloxy-Gly-hippuric acid + L-Phe
show the reaction diagram
-
-
-
ir
carboxypeptidase A5 C-terminus + H2O
?
show the reaction diagram
-
requires an overnight incubation for a partial digestion by CPA4
-
-
?
cathepsin D (138-155) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
chromogranin A (374-388) + H2O
?
show the reaction diagram
-
good substrate
-
-
?
chromogranin A (374-390) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
chromogranin B + H2O
?
show the reaction diagram
-
good substrate
-
-
?
cinnamoyl-L-phenyllactate + H2O
cinnamic acid + L-phenyllactate
show the reaction diagram
-
-
-
ir
clathrin light chain A C-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
dansylglycylglycyl-L-tryptophan + H2O
?
show the reaction diagram
-
assay substrate
-
-
?
des-Asp1-angiotensin + H2O
?
show the reaction diagram
-
partially cleaved in 2 h
-
-
?
dynorphin A8 + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
elongation factor 1 beta 2 N-terminus + H2O
?
show the reaction diagram
-
good substrate
-
-
?
endothelin + H2O
?
show the reaction diagram
-
removal of the C-terminal tryptophan
-
-
?
endothelin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
gamma-actin + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
Gly-L-Tyr + H2O
Gly + L-Tyr
show the reaction diagram
-
-
-
ir
Gly-L-Tyr + H2O
Gly + L-Tyr
show the reaction diagram
-
low activity
-
ir
Gly-L-Tyr + H2O
Gly + L-Tyr
show the reaction diagram
-
low activity
-
ir
Gly-L-Tyr + H2O
Gly + L-Tyr
show the reaction diagram
-
slow substrate
-
-
?
glycyl-L-serylglycyl-L-seryl-N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycyl-L-seryl-L-tryptophan + H2O
glycyl-L-serylglycyl-L-seryl-N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycyl-L-serine + L-tryptophan
show the reaction diagram
-
2,3-diazabicyclo[2.2.2]oct-2-ene-labeled asparagine as a fluorescent amino acid
-
-
?
hippuryl-DL-beta-phenyllactate + H2O
?
show the reaction diagram
-
-
-
?
hippuryl-DL-beta-phenyllactic acid + H2O
hippuric acid + 3-phenyllactic acid
show the reaction diagram
-
-
-
ir
hippuryl-DL-phenylacetic acid + H2O
hippuric acid + DL-phenyllactic acid
show the reaction diagram
-
-
-
ir
hippuryl-DL-phenylalanine + H2O
hippuric acid + DL-phenylalanine
show the reaction diagram
-
-
-
-
?
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
show the reaction diagram
-
-
-
-
?
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
show the reaction diagram
-
-
-
ir
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
show the reaction diagram
-
-
-
ir
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
show the reaction diagram
-
-
-
ir
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
show the reaction diagram
-
-
-
ir
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
show the reaction diagram
-
-
-
ir
hippuryl-DL-phenyllactate + H2O
hippuric acid + DL-phenyllactate
show the reaction diagram
Cephalopina titillator
-
-
-
-
?
hippuryl-DL-phenyllactic acid + H2O
hippuric acid + DL-phenyllactic acid
show the reaction diagram
-
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
show the reaction diagram
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
show the reaction diagram
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
show the reaction diagram
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
show the reaction diagram
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
show the reaction diagram
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
show the reaction diagram
-
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
show the reaction diagram
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
show the reaction diagram
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
show the reaction diagram
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + L-Phe
show the reaction diagram
-
-
-
ir
hippuryl-L-Phe + H2O
hippuric acid + Phe
show the reaction diagram
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + Phe
show the reaction diagram
-
-
-
?
hippuryl-L-Phe + H2O
hippuric acid + L-phenylalanine
show the reaction diagram
-
the hydrolysis of the hippuryl-L-Phe molecule by carboxypeptidase A is investigated using both density functional theory and a hybrid quantum mechanical/molecular mechanical approach. The enzymatic reaction is found to proceed via a promoted water pathway with Glu270 serving as the general base and general acid. Free-energy calculations indicate that the first nucleophilic addition step is rate-limiting, with a barrier of 17.9 kcal/mol. Besides activating the zinc-bound water nucleophile, the zinc cofactor also serves as an electrophilic catalyst that stabilizes the substrate carbonyl oxygen during the formation of the tetrahedral intermediate. In the Michaelis complex, Arg127, rather than Zn(II), is responsible for the polarization of the substrate carbonyl and it also serves as the oxyanion hole
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
show the reaction diagram
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
hippuric acid + L-phenylalanine
show the reaction diagram
-
assay substrate
-
-
?
hippuryl-L-phenylalanine + H2O
?
show the reaction diagram
-
-
-
-
?
hippuryl-Phe + H2O
hippuric acid + Phe
show the reaction diagram
-
-
-
?
hippuryl-Phe + H2O
hippuric acid + Phe
show the reaction diagram
-
-
-
?
hippuryl-Phe + H2O
hippuric acid + Phe
show the reaction diagram
-
-
-
?
kinetensin + H2O
?
show the reaction diagram
-
-
-
-
?
L-beta-phenyllactate-alpha-((2-naphthoyl)amino)-cinnamoyl ester + H2O
L-beta-phenyllactate + alpha-((2-naphthoyl)amino) cinnamate
show the reaction diagram
-
-
-
ir
L-beta-phenyllactate-alpha-(acetylamino)-cinnamoyl ester + H2O
L-beta-phenyllactate + alpha-(acetylamino)cinnamate
show the reaction diagram
-
-
-
ir
L-beta-phenyllactate-alpha-(benzoylylamino)-cinnamoyl ester + H2O
L-beta-phenyllactate + alpha-(benzoylamino)-cinnamate
show the reaction diagram
-
-
-
ir
Leu-enkephalin + H2O
?
show the reaction diagram
-
partially cleaved in 2 h
-
-
?
Leu5-enkephalin + H2O
?
show the reaction diagram
-
-
-
-
?
little SAAS + H2O
?
show the reaction diagram
-
small percentage of cleavage
-
-
?
Met-enkephalin + H2O
?
show the reaction diagram
-
requires an overnight incubation for a partial digestion by CPA4
-
-
?
Met-enkephalin-L-Arg-L-Phe + H2O
Met-enkephalin-L-Arg + L-Phe
show the reaction diagram
-
-
-
-
?
methotrexate-alpha-(1-naphthyl)alanine + H2O
methotrexate + (1-naphthyl)alanine
show the reaction diagram
-
low activity
-
-
?
methotrexate-alpha-phenylalanine + H2O
methotrexate + phenylalanine
show the reaction diagram
-
high activity
-
-
?
N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycyl-L-tryptophan + H2O
N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycine + L-tryptophan
show the reaction diagram
-
2,3-diazabicyclo[2.2.2]oct-2-ene-labeled asparagine as a fluorescent amino acid
-
-
?
N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycylglycyl-L-tryptophan + H2O
N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginylglycylglycine + L-tryptophan
show the reaction diagram
-
2,3-diazabicyclo[2.2.2]oct-2-ene-labeled asparagine as a fluorescent amino acid
-
-
?
N-(2-furanacryoyl)-Phe-Phe + H2O
N-(2-furanacryoyl)-Phe + Phe
show the reaction diagram
-
-
-
ir
N-(3-[2-furyl]acryloyl)-L-Phe-L-Phe + H2O
N-(3-[2-furyl]acryloyl)-L-Phe + L-Phe
show the reaction diagram
-
-
-
-
?
N-(3-[2-furyl]acryloyl)-Phe-Phe
?
show the reaction diagram
Q6ZXB9
-
-
-
?
N-(3-[2-furyl]acryloyl)-Phe-Phe + H2O
?
show the reaction diagram
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
substrate of carboxypeptidase activity assay
-
-
?
N-(4-methoxyphenyl-azoformyl)-L-Phe + H2O
?
show the reaction diagram
Q9UI42
-
-
-
?
N-(4-methoxyphenylazoformyl)-L-phenylalanine + H2O
?
show the reaction diagram
-
-
-
-
?
N-(4-methoxyphenylazoformyl)-Phe-OH + H2O
?
show the reaction diagram
-
substrate for inhibition assay
-
-
?
N-(methoxyphenyl-azoformyl)-Phe-OH + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Gly-L-phenyllactic acid + H2O
N-acetyl-Gly + L-phenyllactic acid
show the reaction diagram
-
-
-
ir
N-acetyl-L-aspartate
acetate + L-aspartate
show the reaction diagram
-
-
-
-
?
N-acetyl-phenylalanyl-L-3-thiaphenylalanine + H2O
?
show the reaction diagram
-
assay substrate
-
-
?
N-carbobenzoxy-Gly-Gly-L-Leu + H2O
N-carbobenzoxy-Gly-Gly + L-Leu
show the reaction diagram
-
-
-
ir
N-carbobenzoxy-Gly-Gly-L-Phe + H2O
N-carbobenzoxy-Gly-Gly + L-Phe
show the reaction diagram
-
-
-
ir
N-carbobenzoxy-Gly-L-Phe + H2O
N-carbobenzoxy-Gly + L-Phe
show the reaction diagram
-
-
-
ir
N-carbobenzoxy-Gly-L-Tyr + H2O
N-carbobenzoxy-Gly + L-Tyr
show the reaction diagram
-
-
-
ir
N-trans-3-(-3-indoleacryloyl)-L-Phe + H2O
N-trans-3-indoleacrylate + L-Phe
show the reaction diagram
-
-
-
ir
N-[3-(2-furyl)acryloyl]-Phe-Phe + H2O
N-[3-(2-furyl)acryloyl]-Phe + Phe
show the reaction diagram
-
-
-
?
N-[3-(2-furyl)acryloyl]-Phe-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
N-[3-(2-furyl)]acryloyl-L-Phe-L-Phe + H2O
N-[3-(2-furyl)]acryloyl-L-Phe + L-Phe
show the reaction diagram
-
-
-
?
N-[4-methoxyphenylazoformyl]-Phe-OH + H2O
?
show the reaction diagram
-
assay substrate
-
-
?
N2acetyl-N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparaginyl-L-tryptophan + H2O
N2-acetyl-N-(2,3-diazabicyclo[2.2.2]oct-2-en-1-ylmethyl)-L-asparagine + L-tryptophan
show the reaction diagram
-
2,3-diazabicyclo[2.2.2]oct-2-ene-labeled asparagine as a fluorescent amino acid
-
-
?
neuromedin N + H2O
?
show the reaction diagram
-
-
-
-
?
neuromedin N + H2O
?
show the reaction diagram
-
good substrate
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
O-(trans-4-chlorocinnamoyl)-L-beta-phenyllactate + H2O
trans-4-chlorocinnamic acid + L-phenyllactic acid
show the reaction diagram
-
-
-
-
?
O-(trans-4-chlorocinnamoyl)-L-phenyllactic acid + H2O
trans-4-chlorocinnamic acid + L-phenyllactic acid
show the reaction diagram
-
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate + H2O
?
show the reaction diagram
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate + H2O
?
show the reaction diagram
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate + H2O
?
show the reaction diagram
-
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-phenylacetic acid + H2O
?
show the reaction diagram
-
-
-
?
O-(trans-p-chlorocinnamoyl)-L-phenyllactic acid + H2O
?
show the reaction diagram
-
-
-
?
O-(trans-p-chlorocinnamyl)-L-beta-phenyllactate + H2O
?
show the reaction diagram
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha + L-beta-phenylalanine
show the reaction diagram
-
-
-
-
?
ochratoxin A + H2O
ochratoxin alpha + L-beta-phenylalanine
show the reaction diagram
Phaffia rhodozyma, Phaffia rhodozyma CBS 5905
-
-
-
-
?
p-nitrophenyl acetate + H2O
nitrophenolate + acetate
show the reaction diagram
-
-
-
-
?
peptidyl-L-amino acid + H2O
?
show the reaction diagram
-
rapid release: Tyr, Phe, Trp, Leu, Ile, Thr, Gln, His, Ala, Val, homoserine, slow release: Asn, Ser, Lys, MetSO2, very slow release: Gly, Asp, Glu, CysSO3, S-carboxymethylcysteine, not released: Pro, hydroxyproline, Arg, enzyme generally releases C-terminal amino acids, with the exception of C-terminal arginine, lysine and proline
-
-
-
peptidylprolyl isomerase A (118-129) + H2O
?
show the reaction diagram
-
good substrate
-
-
?
peptidylprolyl isomerase A (23-39) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
peptidylprolyl isomerase A (26-39) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
peptidylprolyl isomerase A (84-100) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
peptidylprolyl isomerase A (84-92) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
peroxiredoxin V N-terminus + H2O
?
show the reaction diagram
-
good substrate
-
-
?
Phe-Asn-Arg-Pro-Val + H2O
?
show the reaction diagram
Q9UI42
used as substrate in the activity assay
-
-
?
Phe-Asn-Arg-Pro-Val-Asp + H2O
?
show the reaction diagram
Q9UI42
used as substrate in the activity assay
-
-
?
Phe-Asn-Arg-Pro-Val-Val + H2O
?
show the reaction diagram
Q9UI42
used as substrate in the activity assay
-
-
?
procholecystokinin (46-62) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
procholecystokinin (46-63) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
proenkenphalin octapeptide + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
proenkephalin + H2O
?
show the reaction diagram
-
good substrate
-
-
?
propeptidyl-amidating monooxygenase + H2O
?
show the reaction diagram
-
good substrate
-
-
?
proteasome subunit beta type 6 (34-41) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
protein PEN + H2O
?
show the reaction diagram
-
good substrate
-
-
?
protein PEN-20 + H2O
?
show the reaction diagram
-
good substrate
-
-
?
provasopressin (151-end) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
ribosomal protein S21 C-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
sarafotoxin + H2O
?
show the reaction diagram
-
-
-
-
?
sarafotoxin + H2O
?
show the reaction diagram
-
removal of the C-terminal tryptophan
-
-
?
sarafotoxin 6b + H2O
?
show the reaction diagram
-
-
-
-
?
sarafoxin 6b + H2O
?
show the reaction diagram
-
-
-
-
?
secretogranin (287-316) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
secretogranin (300-316) + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
snake venomtoxin + H2O
?
show the reaction diagram
-
-
-
-
?
synaptosomal-associated protein C-terminus + H2O
?
show the reaction diagram
-
good substrate
-
-
?
thioredoxin N-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
vacuolar ATP synthase subunit 2 C-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
vasoconstrictive factor endothelin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
voltage-dependent anion channel protein 1 C-terminus + H2O
?
show the reaction diagram
-
weak substrate
-
-
?
xenopsin + H2O
?
show the reaction diagram
-
-
-
-
?
methotrexate-phenylalanine + H2O
methotrexate + phenylalanine
show the reaction diagram
-
prodrug activation in SW122 cells
-
-
?
additional information
?
-
-
human haemoglobin, removal of specific C-terminal residues
-
-
-
additional information
?
-
-
intermediates of biochemical reaction
-
-
-
additional information
?
-
-
chicken gizzard tropomyosin, effects on interaction between tropomyosin and actomyosin ATPase
-
-
-
additional information
?
-
-
acyl-enzyme intermediates
-
-
-
additional information
?
-
-
the enzyme cleaves C-terminal hydrophobic aliphatic and aromatic residues from other peptides and proteins, not of food in contrast to pancreatic CPA1 and CPA2, for destruction, presumably following the action of chymase
-
-
-
additional information
?
-
-
the enzyme cleaves dipeptides or single amino acids from the C-terminus of polypeptides
-
-
-
additional information
?
-
P15088
the enzyme is a secretory granule metalloexopeptidase, MC-CPA is unique among carboxypeptidases inthaving a CPA-like substrate-binding pocket and enzymatic activity despite overall protein and gene structures more similar to CPB
-
-
-
additional information
?
-
-
CPVL colocalizes with both macrophage-inhibitory protein-1alpha and tumour necrosis factor-alpha
-
-
-
additional information
?
-
-
CPA catalyzes the elimination of the C-terminal amino acid via hydrolysis, with a preference toward residues with hydrophobic side chains
-
-
-
additional information
?
-
-
CPA4 acts as a monocarboxypeptidase
-
-
?
additional information
?
-
-
CPA4 is able to cleave hydrophobic C-terminal residues with a preference for Phe, Leu, Ile, Met, Tyr, and Val. Aliphatic, aromatic, and basic residues in the P1 position have a positive influence on the cleavage specificity. In contrast, acidic residues, Pro, and Gly have a negative influence in the P1 position, neither bradykinin nor des-Arg9-bradykinin or 3-(2-furyl)acryloyl-L-Phe-L-His are substrates for CPA4
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
apolipoprotein B + H2O
?
show the reaction diagram
-
-
-
-
?
endothelin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
hippuryl-L-phenylalanine + H2O
?
show the reaction diagram
-
-
-
-
?
kinetensin + H2O
?
show the reaction diagram
-
-
-
-
?
neuromedin N + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
peptidyl-L-amino acid + H2O
?
show the reaction diagram
-
rapid release: Tyr, Phe, Trp, Leu, Ile, Thr, Gln, His, Ala, Val, homoserine, slow release: Asn, Ser, Lys, MetSO2, very slow release: Gly, Asp, Glu, CysSO3, S-carboxymethylcysteine, not released: Pro, hydroxyproline, Arg, enzyme generally releases C-terminal amino acids, with the exception of C-terminal arginine, lysine and proline
-
-
-
sarafoxin 6b + H2O
?
show the reaction diagram
-
-
-
-
?
snake venomtoxin + H2O
?
show the reaction diagram
-
-
-
-
?
vasoconstrictive factor endothelin 1 + H2O
?
show the reaction diagram
-
-
-
-
?
xenopsin + H2O
?
show the reaction diagram
-
-
-
-
?
methotrexate-phenylalanine + H2O
methotrexate + phenylalanine
show the reaction diagram
-
prodrug activation in SW122 cells
-
-
?
additional information
?
-
-
the enzyme cleaves C-terminal hydrophobic aliphatic and aromatic residues from other peptides and proteins, not of food in contrast to pancreatic CPA1 and CPA2, for destruction, presumably following the action of chymase
-
-
-
additional information
?
-
-
CPA catalyzes the elimination of the C-terminal amino acid via hydrolysis, with a preference toward residues with hydrophobic side chains
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
enhances activation
Cd2+
-
substitution for native Zn, activates apoenzyme
Cd2+
-
activates apoenzyme
Cd2+
-
-
Cd2+
-
efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd; substitution for native Zn, activates apoenzyme
Cd2+
-
efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd
Co2+
-
association constant; substitution for native Zn
Co2+
-
activates apoenzyme
Co2+
-
-
Co2+
-
efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd; substitution for native Zn
Co2+
-
efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd
Co2+
-
X-ray absorption fine study of Co environment in active site, comparison to Zn metalloenzyme
Cu2+
-
-
Mn2+
-
substitution for native Zn
Mn2+
-
activates apoenzyme
Mn2+
-
-
Mn2+
-
efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd; substitution for native Zn
Ni2+
-
substitution for native Zn
Ni2+
-
activates apoenzyme
Ni2+
-
-
Ni2+
-
efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd; substitution for native Zn
Ni2+
-
efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd
Zn2+
-
1 mol Zn per mol of enzyme; His-69, Glu-72 and His-196 bind Zn to carboxypeptidase; metalloenzyme; required; Zn ligand is His, Zn involved in both binding and catalysis
Zn2+
-
required
Zn2+
-
1 mol Zn bound to a single polypeptide, acts as electrophilic catalyst; metalloenzyme
Zn2+
-
activates apoenzyme
Zn2+
-
0.98-1.03 mol Zn per mol enzyme; metalloenzyme
Zn2+
-
-
Zn2+
-
1 mol Zn per mol of enzyme; metalloenzyme
Zn2+
-
1,01 mol Zn per mol enzyme; 1 mol Zn per mol of enzyme; metalloenzyme
Zn2+
-
metalloenzyme
Zn2+
-
0.91-1.07 mol Zn per mol enzyme; 1 mol Zn per mol of enzyme; metalloenzyme
Zn2+
-
1.01 mol Zn per mol enzyme; 1 mol Zn per mol of enzyme; metalloenzyme
Zn2+
-
role of Tyr249 in Zn binding discussed
Zn2+
-
Zn binding mechanism
Zn2+
-
crystallographic study of Zn environment; metalloenzyme
Zn2+
-
-
Zn2+
-
Zn enhances kinetic inhibition by imidazole 560fold due to formation of ternary complexes with enzyme
Zn2+
-
X-ray absorption fine study of Zn environment in active site, comparison to Co metalloenzyme
Zn2+
-
binds and stabilizes the active site
Zn2+
-
required
Zn2+
Q8AXN4
zinc-metallopeptidase, binding residues are H69, E72, and H196
Zn2+
-
zinc metalloprotease
Zn2+
-
zinc-metallopeptidase
Zn2+
P15088
zinc metallopeptidase, binding site
Zn2+
-
metalloenzyme, the amount of zinc excreted by the pancreas is related to enzyme output, quantitative determination, overview
Zn2+
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
a zinc binding site is indentified by sequence analysis of cDNA clones; a zinc binding site is indentified by sequence analysis of cDNA clones; a zinc binding site is indentified by sequence analysis of cDNA clones; a zinc binding site is indentified by sequence analysis of cDNA clones; a zinc binding site is indentified by sequence analysis of cDNA clones; a zinc binding site is indentified by sequence analysis of cDNA clones; a zinc binding site is indentified by sequence analysis of cDNA clones
Zn2+
-
contains a zinc-containing hydrolase fold
Zn2+
-
zinc-dependent enzyme
Zn2+
-
; carboxypeptidase A is a zinc-containing enzyme
Zn2+
-
zinc metalloenzyme
Zn2+
-
zinc-dependent exoprotease
Mn2+
-
efficiency of metals in decreasing order: Zn, Co, Ni, Mn, Cd
additional information
-
metallocarboxypeptidase
additional information
-
metalloprotease
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+-)-2-benzylsuccinic acid
-
-
(2E)-2-mercapto-3-phenylacrylic acid
-
-
(2E)-2-mercapto-4-phenylbut-2-enoic acid
-
-
(2E)-2-mercapto-5-phenylpent-2-enoic acid
-
-
(2R,3S)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
-
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
-
(2R,4S)-2-benzyl-3-methanesulfinylpropanoic acid
-
-
(2S)-2-([hydroxy[(1R)-1-[[1-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-prolyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IPro2
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-b-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. I-beta-Ala2
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IAla2
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-phenylalanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IPhe2
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IGly2
(2S)-2-([hydroxy[(1S)-1-[[1-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-prolyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IPro1
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-b-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. I-beta-Ala1
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IAla1
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-phenylalanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IPhe1
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
i.e. IGly1
(2S)-2-[(hydroxy[(1R)-1-[(1,4,7,10-tetraazacyclododecan-1-ylacetyl)amino]ethyl]phosphoryl)oxy]-3-phenylpropanoic acid
-
i.e. I2
(2S,3R)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
-
(2S,3R)-2-benzyl-3,4-epoxybutanoic acid
-
-
(2S,4R)-2-benzyl-3-methanesulfinylpropanoic acid
-
-
(2S,4S)-2-benzyl-3-methanesulfinylpropanoic acid
-
-
(R)-2-benzyl-3-(4-methoxybenzoyl)propanoic acid
-
a ketoester substrate analogue
(R)-2-benzyl-3-(methylthio)propanoic acid
-
-
(R)-2-benzyl-3-(N-sulfamoyl)aminopropanoic acid
-
-
(R)-2-benzyl-3-nitropropanoic acid
-
; X-ray crystallography discloses that the nitro group well mimics the transition state occurred in the hydrolysis catalyzed by CPA, that is, an O,O'-bidentate coordination to the zinc ion and the two respective hydrogen bonds with Glu-270 and Arg-127. Because the nitro group is a planar species, (R)-2-benzyl-3-nitropropanoic acid is as a pseudo-transition-state analog inhibitor against CPA
(R)-2-benzyl-5-nitro-4-oxopentanoic acid
-
-
(R)-2-mercaptomethyl-2-methyl-3-phenylpropanoic acid
-
-
(R)-hippuryl-alpha-MePhe
-
-
(R)-N-(2-chloroethyl)-N-methylphenylalanine
-
-
(R)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(R)-N-benzylcysteine
-
-
(R)-N-cyclohexylcysteine
-
-
(R)-N-formyl-N-hydroxyphenylalanine
-
-
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
competitive
(R)-N-isopropylcysteine
-
-
(R)-N-phenethylcysteine
-
-
(R)-N-sulfamoylphenylalanine
-
competitive
(R)-N-sulfamoylphenylalanine
-
-
(R,S)-2-benzyl-5-nitro-4-oxopentanoic acid
-
-
-
(R,S)-3-phenyl-2-sulfamoyloxypropionic acid
-
competitive
(R,S)-N-(hydroxyaminocarbonyl)-phenylalanine
-
competitive
(R,S)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(R,S)-N-sulfamoylphenylalanine
-
competitive
(RS)-2-benzyl-3-(methylthio)propanoic acid
-
-
(RS)-2-benzyl-3-nitropropanoic acid
-
-
(RS)-2-benzyl-3-sulfamoylpropionic acid
-
-
(RS)-2-isobutyl-3-nitropropanoic acid
-
-
(RS)-2-mercaptomethyl-2-methyl-3-phenylpropanoic acid
-
-
(RS)-2-mercaptomethyl-2-methylbutanoic acid
-
-
(RS)-2-mercaptomethylbutyric acid
-
-
(RS)-3-phenyl-2-sulfamoyloxypropionic acid
-
competitive
(RS)-N-(hydroxyaminocarbonyl)-phenylalanine
-
-
(RS)-N-formyl-N-hydroxyphenylalanine
-
-
(RS)-N-sulfamoylphenylalanine
-
-
(S)-2-(Hydroxy-[(S)-1-[(S)-3-methyl-2-(2-1,4,7,10tetraaza-cyclododec-1-yl-acetylamino)-pentanoylamino]-ethyl]-phosphinoyloxy)-3-phenyl-propionic acid
-
i.e. IIle1; i.e. IIle2
(S)-2-benzyl-3-(methylthio)propanoic acid
-
-
(S)-2-benzyl-3-(N-sulfamoyl)aminopropanoic acid
-
-
(S)-2-benzyl-3-nitropropanoic acid
-
-
(S)-2-benzyl-5-nitro-4-oxopentanoic acid
-
-
(S)-N-(2-chloroethyl)-N-methylphenylalanine
-
-
(S)-N-(N-benzylsulfamoyl)phenylalanine
-
-
(S)-N-(N-hydroxysulfamoyl)phenylalanine
-
competitive
(S)-N-(N-isopropylsulfamoyl)phenylalanine
-
-
(S)-N-(N-methylsulfamoiyl)phenylalanine
-
-
(S)-N-(N-phenylethylsulfamoyl)phenylalanine
-
-
(S)-N-benzylcysteine
-
-
(S)-N-cyclohexylcysteine
-
-
(S)-N-formyl-N-hydroxyphenylalanine
-
-
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
competitive
(S)-N-isopropylcysteine
-
-
(S)-N-methyl-N-sulfamoylphenylalanine
-
-
(S)-N-phenethylcysteine
-
-
(S)-N-sulfamoylphenylalanine
-
-
(S)-N-sulfamoylphenylalanine
-
competitive
(S)-N-sulfamoylphenylalanine benzyl ester
-
pH 7.5
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
complete inhibition at 10 mM
1,10-phenanthroline
-
80% inhibition at 0.1 mM
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
complete inhibition at 1 mM
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
2-(1-Carboxy-2-phenyl ethyl)-4,6-dichlorophenol
-
-
2-(1-Carboxy-2-phenylethyl)-4-phenylazophenol
-
-
2-(1-Carboxy-2-phenylethyl)phenol
-
-
2-(1-hydroxy-5-oxopyrrolidin-2-yl)-3-phenylpropanoic acid
-
-
2-benzyl-3,4-epithiobutanoic acid
-
-
2-benzyl-3,4-epoxybutanoic acid
-
-
2-benzyl-3-iodo-propanoic acid
-
mechanisms elucidated from complex with inactivator
2-benzyl-3-mecaptopropionate
-
Ki: 11 nM
2-benzyl-3-[(difluoroacetyl)(hydroxy)amino]propanoic acid
-
-
2-benzyl-3-[(fluoroacetyl)(hydroxy)amino]propanoic acid
-
-
2-benzyl-3-[formyl(hydroxy)amino]propanoic acid
-
-
2-benzyl-3-[hydroxy(methoxyacetyl)amino]propanoic acid
-
-
2-benzyl-3-[hydroxy(methoxycarbonyl)amino]propanoic acid
-
-
2-benzyl-3-[hydroxy(trifluoroacetyl)amino]propanoic acid
-
-
2-benzyl-4-oxopentanoic acid
-
-
2-benzyl-5,5,5-trifluoro-4-oxopentanoic acid
-
-
2-benzyl-5-bromo-4-oxopentanoic acid
-
-
2-benzylsuccinic acid
-
potent inhibitor
3-hydroxyaminocarbonyl-2-benzylpropanoic acid
-
-
3-Phenylpropionic acid
-
Ki: 0.062-0.19 mM
3-Phenylpropionic acid
-
-
3-Phenylpropionic acid
-
Ki: 0.062 mM
3-Phenylpropionic acid
-
Ki: 0.81 mM, noncompetitive
3-Phenylpropionic acid
-
84% inhibition at 1 mM, some derivatives also inhibitory
3-Phenylpropionic acid
-
-
3-Phenylpropionic acid
-
-
3-Phenylpropionic acid
-
Ki: 6.1 mM
3-Phenylpropionic acid
-
noncompetitive, Ki: 0.12 mM
3-Phenylpropionic acid
-
Ki: 0.482 mM
3-[acetyl(hydroxy)amino]-2-benzylpropanoic acid
-
-
4-Phenylbutyric acid
-
Ki: 0.118 mM
8-hydroxyquinoline
-
-
alpha-benzyl-2-oxo-1,3-oxazolidine-4-acetic acid
-
all four stereoisomers inhibit in a time dependent manner, inhibited enzyme does not regain its enzymatic activity upon dialysis, inactivation is prevented by 2-benzylsuccinic acid
-
alpha-benzyl-2-oxo-1,3-oxazolidine-5-acetic acid
-
irreversible
-
aminobenzylsuccinic acid
-
Ki: 0.039 mM
-
anilino(mercapto)acetic acid
-
-
Ascaris carboxypeptidase inhibitor
-
-
-
benzylsuccinate
-
-
Benzylsuccinic acid
-
-
Benzylsuccinic acid
-
Ki: 0.0016
Benzylsuccinic acid
-
Ki: 450 nM
Carbobenzoxyglycine
-
-
Carbobenzoxyglycine
-
activator of dipeptide hydrolysis, inhibitor of tripeptide hydrolysis, Ki: 27 mM
CBZ-Ala-Gly-PSI[P(O2)O]-Phe
-
crystallographic study of structure Ki: 0.710 nM
CBZ-Phe-Val-PSI[P(O2)O]-Phe
-
crystallographic study of structure Ki: 0.000011 nM
Cd2+
-
decreases carboxypeptidase A activity probably due to the direct inhibition by the metal
Cd2+
-
about 30% inhibition in small intestine in vivo
CdCl2
-
55% inhibition at 1 mM
Chelating agents
-
-
Chelating agents
-
-
Chelating agents
-
-
Chelating agents
-
-
Chelating agents
-
-
Chelating agents
-
-
chitosan citrate
-
-
chitosan hydrochloride
-
-
cinnamate
-
Ki: 5 mM
citrate
-
-
CN-
-
-
Co(II)-cyclen complex
-
-
Cu(II)-cyclen complex
-
-
Cu2+
-
-
CuCl2
-
complete inhibition at 1 mM
Cys
-
-
D-Cys
-
binds tightly to the active site zinc. D-Cys binds the active site zinc with a sulfur ligand and forms additional interactions with surrounding side chains of the enzyme. D-Cys binding induces a concerted motion of the side chains around the sinc ion
D-His
-
Ki: 20 mM
D-N-(hydroxyaminocarbonyl)phenylalanine
-
-
D-N-hydroxyaminocarbonyl phenylalanine
-
-
D-penicillamine
-
-
D-penicillamine
-
catalyzes Zn2+ transfer from carboxypeptidase A to chelators, catalytic chelation
D-Phe
-
Ki: 2 mM
D-Phe
-
-
D-Phe
-
Ki: 0.074 mM
D-Trp
-
Ki: 0.014 mM
DL-benzylsuccinic acid
-
-
DTT
-
52% inhibition at 1 mM
EDTA
-
-
EDTA
-
complete inhibition at 10 mM
EDTA
-
-
EDTA
-
86% inhibition at 1 mM
EDTA
-
; 10 mM
EDTA
Q6ZXB9
10 mM strongly inhibits
EDTA
-
complete inhibition of CPA4 activity s only achieved using a 100 mM concentration of EDTA in an overnight incubation, whereas the same inhibitor concentration causes only 60% inhibition after 5 h of treatment
endoglycosidase H
-
lowers CPVL expression in monocyte-derived macrophages
-
Fe3+
-
-
Gly-Asn-Arg-Pro-Thr
Q9UI42
-
Gly-Asn-Arg-Pro-Val-Thr
Q9UI42
-
Gly-L-Tyr
-
-
Gly-L-Tyr
-
Ki: 0.1 mM
HgCl2
-
80% inhibition at 10 mM
hydroxyalkylphosphinyl L-beta-phenyllactate ester
-
binds to the active site
Hydroxyquinoline sulfonate
-
-
Hydroxyquinoline sulfonate
-
-
imidazole
-
Zn2+ enhances kinetic inhibition by imidazole 560fold due to formation of ternary complexes with enzyme
indole acetic acid
-
Ki: 0.078 mM
indole acetic acid
-
-
indole acetic acid
-
noncompetitive, Ki: 0.17 mM
L-beta-Phenyllactate
-
product inhibtion
L-Lys-L-tyrosineamide
-
-
L-N-(aminocarbonyl)phenylalanine
-
-
L-N-(hydroxyaminocarbonyl)phenylalanine
-
-
L-N-hydroxyaminocarbonyl phenylalanine
-
-
L-Penicillamine
-
-
L-Phe
-
-
L-Phe-phosphoramidate-phenylester
-
Ki: 0.0021 mM
L-Phenyllactate
-
Ki: 0.058 mM
latexin
-
a carboxypeptidase A inhibitor protein, inhibits mast-cell CPA, CPA1, and CPA2, is associated with granular structures distinct from secretory granules and lysosomes in peritoneal mast cells, purification from and expression analysis in peritoneal mast cell granules, overview; a carboxypeptidase A inhibitor protein, inhibits mast-cell CPA, CPA1, and CPA2, is associated with intracellular granular structures distinct from MCCPA- and histamine-containing secretory granules and lysosomes in peritoneal mast cells, purification from and expression analysis in peritoneal mast cell granules, overview
-
latexin
-
cloned from human brain and expressed in Escherichia coli, CPA4-latexin complex structure determination and analysis
-
latexin
-
from mouse recombinantly expressed as His-tagged enzyme in Escherichia coli and purified, overview, analysis of complex formation with CPAI, overview
-
latexin
-
-
-
latexin
-
-
-
latexin
-
-
-
leech carboxypeptidase inhibitor
-
LCI, tight-binding, competitive inhibition, the inhibitor contains four disulfide bonds, biding structure with CPA, oxidative folding pathway and intermediate of wild-type and mutant C19A/C43A mutant, determination of thermodynamics and conformational stability of wild-type and mutant enzymes at pH 8.4/high concentration of DTT, overview
-
leech carboxypeptidase inhibitor
-
LCI
-
leech carboxypeptidase inhibitor
-
-
-
mercapto(methylamino)acetic acid
-
-
N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl-N-[(1R)-1-[[(1S)-1-carboxy-2-phenylethoxy](hydroxy)phosphoryl]ethyl]glycinamide
-
i.e. IGlyGly2
N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl-N-[(1S)-1-[[(1S)-1-carboxy-2-phenylethoxy](hydroxy)phosphoryl]ethyl]glycinamide
-
i.e. IGlyGly1
N-(2-chloroethyl)-N-methylphenylalanine
-
both enantiomers, computational analysis of the mechanism for reactive inhibition, quantum mechanical and molecular mechanical methods, the inhibitor enantiomers both bind at the active site and perform nucleophilic deactivation involving cofactor Zn2+, overview
N-(3-chloropropionyl)-L-phenylalanine
-
-
N-(hydroxyacetyl)-Phe
-
irreversible inactivation, Kinact/Ki: 71 M-1s-1
-
N-Bromoacetyl-N-methyl-L-phenylalanine
-
rapid inactivation
N-glycosidase
-
lowers CPVL expression in monocyte-derived macrophages
-
N-phenylphosphoryl-L-phenylalanine
-
Ki: 0.0021 mM
O-(hydroxyacetyl)-beta-phenyllactate
-
irreversible inactivation, Kinact/Ki: 57 M-1s-1
o-phenanthroline
Q6ZXB9
1 mM strongly inhibits
O-[[(1R)-(N-phenylmethoxycarbonyl)-L-alanyl]aminoethyl]hydroxyphosphinyl-L-3-phenyllactate
-
-
p-iodo-beta-phenylpropionate
-
-
p-Nitrophenylacetic acid
-
Ki: 2.5 mM
P2O74-
-
-
Pb2+
-
-
Phe phosphonate
-
Ki: 0.001 mM
Phe-Asn-Arg-Ala-Val-Asp
Q9UI42
-
Phe-Asn-Arg-Ala-Val-Val
Q9UI42
-
Phe-Asn-Arg-Pro-Val
Q9UI42
-
Phe-Asn-Arg-Pro-Val-Asp
Q9UI42
-
Phe-Asn-Arg-Pro-Val-Val
Q9UI42
-
phenylacetic acid
-
Ki: 0.39 mM
phenylacetic acid
-
noncompetitive, Ki: 0.73 mM
PO43-
-
-
polypeptide inhibitor
-
molecular weight 10000, Ki: 1 nM
-
Potato carboxypeptidase inhibitor
-
-
-
Potato carboxypeptidase inhibitor
-
Ki: 2 nM
-
Potato carboxypeptidase inhibitor
-
molecular weight 38000, detailed study of inhibitor effects, stability, physical properties, purification protocol
-
Potato carboxypeptidase inhibitor
-
Ki: 5 nM
-
Potato carboxypeptidase inhibitor
-
Ki: 107 nM
-
Potato carboxypeptidase inhibitor
-
-
-
Potato carboxypeptidase inhibitor
-
i.e. PCI, wild-type and several mutants, oxidative folding, hydrogen exchange, and conformational stability, overview, secondary contact binding site structure and mechanism dependent, recombinant expression of the inhibitor protein in Escherichia coli, overview, steady-state binding kinetics
-
Potato carboxypeptidase inhibitor
-
-
-
Potato carboxypeptidase inhibitor
-
PCI
-
Potato carboxypeptidase inhibitor
-
PCI
-
Potato carboxypeptidase inhibitor
-
-
-
potato carboxypeptidase inhibitor mutant DELTA37-39
-
-
-
potato carboxypeptidase inhibitor mutant DELTA38-39
-
-
-
potato carboxypeptidase inhibitor mutant DELTA39
-
-
-
potato carboxypeptidase inhibitor mutant G39F
-
-
-
potato carboxypeptidase inhibitor mutant P36G
-
-
-
potato carboxypeptidase inhibitor mutant V38G
-
-
-
potato carboxypeptidase inhibitor mutant Y37F
-
-
-
potato carboxypeptidase inhibitor mutant Y37G
-
-
-
potato tuber carboxypeptidase inhibitor
-
95% inhibition at 0.001 mM
-
Proteins from Ascaris lumbricoides
-
molecular weight 7600, Ki in nM range, extensive structural analysis of inhibitors
-
rac-2-(mercaptomethyl)-3-cyclohexylpropanoic acid
-
-
rac-2-(mercaptomethyl)-4-methylpentanoic acid
-
-
rac-2-(mercaptomethyl)-6-phenylhexanoic acid
-
-
rac-2-benzyl-3-mercaptopropanoic acid
-
-
rac-2-benzyl-5-chloropentanoic acid
-
-
rac-N-(1-naphthylmethyl)cysteine
-
-
rac-N-(aminocarbonyl)phenylalanine
-
-
rac-N-(cyclohexylmethyl)cysteine
-
-
rac-N-(hydroxyaminocarbonyl)phenylalanine
-
-
rac-N-(p-methoxy)benzylcysteine
-
-
rac-N-benzyl-N-methylcysteine
-
-
rac-N-benzylcysteine
-
-
rac-N-cyclohexylcysteine
-
-
rac-N-ethylcysteine
-
-
rac-N-isobutylcysteine
-
-
rac-N-isopropylcysteine
-
-
rac-N-phenethylcysteine
-
-
rac-N-phenylpropylcysteine
-
-
rac-N-propylcysteine
-
-
SH-
-
-
SR48692
-
-
thioglycolate
-
-
thiolactate
-
-
-
threo-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
-
tick carboxypeptidase inhibitor
-
i.e. TCI, a 75 amino acid, two-domain protein from the blood-sucking tick Rhipcephalus bursa, recombinantly expressed in Escherichia coli and purified, three-dimensional structure of the enzyme-inhibitor protein complex, inhibitor binding and inhibition mechanism, overview
-
tick carboxypeptidase inhibitor
-
TCI
-
tick carboxypeptidase inhibitor
-
from Rhipicephalus bursa
-
Zn2+
-
effect of pH on Zn inhibition, ZnOH+ is inhibitory in vivo
Zn2+
Q6ZXB9
at 0.1 mM 27.5% activity relative to control
mercaptoacetyl-D-Phe
-
Ki: 220 nM
additional information
-
substrate inhibition by: carbobenzoxy-Glyl-L-Phe, benzoyl-Gly-Phe
-
additional information
-
dramatic excess substrate inhibition
-
additional information
-
comparison of Ki-values of enzyme crystals and solution
-
additional information
-
enzyme acetylation reduces activity by 97%
-
additional information
-
study of pH-dependence of inhibition
-
additional information
-
study about coordination of low molecular weight inhibitors to metal ion
-
additional information
-
analysis of interactions between enzyme and multiple inhibitors using combination plots
-
additional information
-
mechanic strain may modify effect of inhibitors
-
additional information
-
molecular dynamics characterization of inhibitor adducts and structural variations induced by inhibitors
-
additional information
-
pH-dependent properties of Co enzymeL-Phe complexes
-
additional information
-
no inhibition by erythro-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
additional information
-
no inhibition by (2R,4R)-2-benzyl-3-methanesulfinylpropanoic acid
-
additional information
-
sulfamide derivatives as transition state analogue inhibitors for carboxypeptidase A, synthesis, overview
-
additional information
-
no inhibition by N-(aminocarbonyl)phenylalanine up to 3.6 mM
-
additional information
-
synthesis of cyclen-containing inhibitors specific for CPA
-
additional information
-
rational design of mechanism-based irreversible enzyme inhibitors, inhibition mechanism, overview
-
additional information
-
no or poor inhibition by soybean Kunitz trypsin inhibitor, E64, leupeptin, chymostatin, pepstatin A, N-tosyl-L-lysine chloromethyl ketone, N-tosyl-L-phenylalanine chloromethyl ketone, iodoacetic acid
-
additional information
-
feeding of the laravae on broccoli foliage reduces the enzyme activity in the midgut
-
additional information
-
no inhibition by pyrantel tartrate, 12.5% in the anthelmintic drug Banminth
-
additional information
Q6ZXB9
PMSF at 2 mM, E-64 at 0.001 mM and Mn2+, Ni2+, Ca2+ and Mg2+ at 1 mM have no effect on activity
-
additional information
-
O-glycosidase has no effect in monocyte-derived macrophages. CPVL in THP-1 and Jurkat cell lines are insensitive to treatment with a cocktail of O-glycosidase, N-glycosidase and endoglycosidase H
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
carbobenzoxy-Gly-L-Phe
-
substrate inhibition
Chymotrypsin
-
activates
-
phorbol myristate acetate
-
-
Proteoglycan
-
there is evidence indicating that the processing of pro-MC-CPA into active protease is dependent on proteoglycan
-
Soybean trypsin inhibitor
-
leads to increased carboxypeptidase activity in larval midgut
-
Trypsin
-
activates
-
Trypsin
Q9UI42
activates zymogen
-
Trypsin
-
procarboxypeptidase A, pro CPA, is converted into the active form of CPA by trypsin
-
Trypsin
-
tryptic activation at a 1:10 (w/w) ratio for 60 min at room temperature
-
Co2+
Q6ZXB9
stimulates, at 1 mM 168% activity relative to control
additional information
-
-
-
additional information
-
substrate activation by some substrates
-
additional information
-
activation by chymotrypsin and trypsin
-
additional information
Q8AXN4
the triad for binding of the activation peptide consists of Asp, Phe, and Trp residues
-
additional information
-
the capacity of poloxamer 188 to suppress aggregation of denaturated carboxypeptidase A is compared to that of polyethylenglycol
-
additional information
-
infection with Ptf1a-expressing adenovirus vector induces the expression of the gene for carboxypeptidase in Pdx-1-positive pancreatic duct-derived (PPPD) cells
-
additional information
-
lipopolysaccharide has no effect on expression in monocyte-derived dendritic cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.313
(S)-hippuryl-alpha-MePhe
-
pH 7.5
0.344
(S)-hippuryl-alpha-methylphenyllactic acid
-
pH 7.5
0.072
(S)-hippuryl-OPhe
-
pH 7.5
0.372
3-(2-furyl)acryloyl-L-Phe-L-Ala
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.0233
3-(2-furyl)acryloyl-L-Phe-L-Ile
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.0194
3-(2-furyl)acryloyl-L-Phe-L-Leu
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.04
3-(2-furyl)acryloyl-L-Phe-L-Met
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.0556
3-(2-furyl)acryloyl-L-Phe-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.0615
3-(2-furyl)acryloyl-L-Phe-L-Trp
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.0573
3-(2-furyl)acryloyl-L-Phe-L-Val
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.0135
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-Phe
-
-
-
0.0016
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-AlaL-beta-phenyllactate
-
-
-
0.22
Ac-Phe-ThiaPhe
-
-
0.227
angiotensin I
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.78
angiotensin I
-
-
0.1
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
-
1
benzoyl-Gly-Gly-Phe
-
-
0.2
benzoyl-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
-
0.23
benzoyl-Gly-L-Phe
-
at 0.1-0.4 mM substrate
0.45
benzoyl-Gly-L-Phe
-
-
0.8 - 11
benzoyl-Gly-L-Phe
-
-
10
benzoyl-Gly-L-Phe
-
at 1-10 mM substrate
0.051 - 0.088
benzoyl-Gly-phenyllactate
-
-
0.14
Benzyloxycarbonyl-Ala-Phe
-
-
0.31
Benzyloxycarbonyl-Gly-Phe
-
-
0.23
Benzyloxycarbonyl-Phe-Leu
-
-
0.74
Carbobenzoxy-Gly-Gly-Leu
-
-
1.34
Carbobenzoxy-Gly-Gly-Phe
-
-
2.11
carbobenzoxy-Gly-Gly-Val
-
-
0.16
carbobenzoxy-Gly-L-Leu
-
-
33
carbobenzoxy-Gly-L-Leu
-
mixture of isoenzyme 2 and 3
0.21
carbobenzoxy-Gly-L-Phe
-
-
0.71
carbobenzoxy-Gly-L-Phe
-
-
1.95 - 37
carbobenzoxy-Gly-L-Phe
-
-
2 - 37
carbobenzoxy-Gly-L-Phe
-
-
3
carbobenzoxy-Gly-L-Phe
-
at 1-4 mM substrate
13.3
carbobenzoxy-Gly-L-Phe
-
at 4-40 mM substrate
16.1
carbobenzoxy-Gly-L-Phe
-
mixture of isoenzyme 2 and 3
6.1 - 7.2
carbobenzoxy-Gly-L-Trp
-
-
14.3
carbobenzoxy-Gly-L-Trp
-
mixture of isoenzyme 2 and 3
0.15 - 0.19
cinnamoyl-L-phenyllactate
-
-
0.7
Gly-L-Tyr
-
-
0.02
hippuryl-DL-beta-phenylacetic acid
-
-
780
hippuryl-DL-beta-phenyllactate
-
pH 7.5, 25C, mutant enzyme Y248F
1300
hippuryl-DL-beta-phenyllactate
-
pH 7.5, 25C, wild-type enzyme
0.15
hippuryl-DL-phenyllactate
-
-
0.2
hippuryl-L-Arg
-
-
0.33
hippuryl-L-Phe
-
-
0.41
hippuryl-L-Phe
-
-
0.81 - 11
hippuryl-L-Phe
-
-
1.07
hippuryl-L-Phe
-
soluble enzyme
1.65
hippuryl-L-Phe
-
immobilized enzyme
2.7
hippuryl-L-Phe
-
-
3.3
hippuryl-L-Phe
-
pH 7.5, 25C, mutant enzyme Y248A
5.6
hippuryl-L-Phe
-
pH 7.5, 25C, mutant enzyme Y248F
60
hippuryl-L-Phe
-
pH 7.5, 25C, wild-type enzyme
0.075
hippuryl-L-phenylalanine
-
pH 7.4, 25C, recombinant enzyme
0.062
hippuryl-L-phenyllactate
-
-
0.11
hippuryl-L-phenyllactate
-
-
0.11
hippuryl-L-phenyllactate
-
mixture of isoenzyme 2 and 3
0.7
hippuryl-Phe
-
pH 7.5
0.000124
L-beta-phenyllactate-alpha-((2-naphthoyl)amino)-cinnamoyl ester
-
-
0.0124
L-beta-phenyllactate-alpha-(acetylamino)-cinnamoyl ester
-
-
0.000223
L-beta-phenyllactate-alpha-(benzoylylamino)-cinnamoyl ester
-
-
0.165
Leu-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.55
Met-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.00923
Met-enkephalin-L-Arg-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.065
methotrexate-alpha-(1-naphthyl)alanine
-
pH 7.4, 25C, recombinant enzyme
0.1
N-(2-furanacryoyl)-Phe-Phe
-
-
-
0.024
N-(3-[2-furyl]acryloyl)-Phe-Phe
Q6ZXB9
in the absence of Co2+
0.034
N-(3-[2-furyl]acryloyl)-Phe-Phe
Q6ZXB9
in the presence of Co2+
0.44
N-acetyl-Gly-L-phenyllactic acid
-
-
0.74
N-carbobenzoxy-Gly-Gly-L-Leu
-
carboxypeptidase 1
6.53
N-carbobenzoxy-Gly-Gly-L-Leu
-
carboxypeptidase 2
0.0346
N-carbobenzoxy-Gly-Gly-L-Phe
-
carboxypeptidase 1
0.314
N-carbobenzoxy-Gly-Gly-L-Phe
-
carboxypeptidase 2
0.0449
N-carbobenzoxy-Gly-L-Phe
-
carboxypeptidase 1
0.985
N-carbobenzoxy-Gly-L-Phe
-
carboxypeptidase 2
0.143
N-carbobenzoxy-Gly-L-Tyr
-
carboxypeptidase 1
0.145
N-carbobenzoxy-Gly-L-Tyr
-
carboxypeptidase 2
0.05
N-trans-3-(-3-indoleacryloyl)-L-Phe
-
-
27
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25C, mutant enzyme Y248A
76
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25C, mutant enzyme Y248F
340
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25C, wild-type enzyme
0.000329
neurotensin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.49
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25C, mutant enzyme Y248A
5.8
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25C, mutant enzyme Y248F
120
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25C, wild-type enzyme
0.5
ochratoxin A
-
-
1.1
ochratoxin A
-
-
0.0043
methotrexate-alpha-phenylalanine
-
pH 7.4, 25C, recombinant enzyme
additional information
additional information
-
dissociation constant of enzyme GlyTyr complex: 0.001, no Michaelis-Menten kinetics with some substrates, larger substrates tend to have smaller Km-values than smaller substrates
-
additional information
additional information
-
derivation from classical Michalis-Menten kinetics with some substrates
-
additional information
additional information
-
-
-
additional information
additional information
-
approximations for several substrates: 0.01 mM
-
additional information
additional information
-
comparison of Km-values in crystals and in solution; comparison of Km-values of enzyme crystals and solution
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
comparison of affinities of various substituted metalloenzymes
-
additional information
additional information
-
-
-
additional information
additional information
-
Km values of immobilized enzyme generally higher than those in solution
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
100
(Ala)4
-
-
0.33
(S)-hippuryl-alpha-MePhe
-
pH 7.5
477
(S)-hippuryl-alpha-methylphenyllactic acid
-
pH 7.5
682
(S)-hippuryl-OPhe
-
pH 7.5
24.3
3-(2-furyl)acryloyl-L-Phe-L-Ala
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
12.4
3-(2-furyl)acryloyl-L-Phe-L-Ile
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
13.4
3-(2-furyl)acryloyl-L-Phe-L-Leu
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
23.9
3-(2-furyl)acryloyl-L-Phe-L-Met
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
44.3
3-(2-furyl)acryloyl-L-Phe-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
57.3
3-(2-furyl)acryloyl-L-Phe-L-Trp
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
19.4
3-(2-furyl)acryloyl-L-Phe-L-Val
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.062
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-L-beta-phenyllactate
-
-
-
1.18
5-dimethyl-aminonaphthalene-1-sulfonyl-Ala-Ala-Phe
-
-
-
8.23
angiotensin I
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
767
benzoyl-Gly-Gly-L-alpha-hydroxy-beta-phenyllactate
-
-
-
13.3
benzoyl-Gly-Gly-L-Phe
-
-
20
benzoyl-Gly-Gly-Phe
-
-
505
benzoyl-Gly-L-alpha-hydroxy-betaphenyllactate
-
-
-
11.7
benzoyl-Gly-L-Phe
-
at 0.1-0.4 mM substrate
16
benzoyl-Gly-L-Phe
-
-
66.7
benzoyl-Gly-L-Phe
-
at 1-10 mM substrate
93.3 - 183
benzoyl-Gly-L-Phe
-
-
467 - 583
benzoyl-Gly-phenyllactate
-
-
89
Benzyloxycarbonyl-Ala-Phe
-
-
4.2
Benzyloxycarbonyl-Gly-Phe
-
-
66
Benzyloxycarbonyl-Phe-Leu
-
-
85
carbobenzoxy-Gly-Gly-L-Tyr
-
-
5.02
Carbobenzoxy-Gly-Gly-Leu
-
-
11.9
Carbobenzoxy-Gly-Gly-Phe
-
-
6.13
carbobenzoxy-Gly-Gly-Val
-
-
29
carbobenzoxy-Gly-L-Leu
-
mixture of isoenzyme 2 and 3
14.7
carbobenzoxy-Gly-L-Phe
-
-
48.3
carbobenzoxy-Gly-L-Phe
-
at 1-4 mM substrate
90 - 198
carbobenzoxy-Gly-L-Phe
-
-
91.7 - 200
carbobenzoxy-Gly-L-Phe
-
-
112
carbobenzoxy-Gly-L-Phe
-
at 4-40 mM substrate
139
carbobenzoxy-Gly-L-Phe
-
mixture of isoenzyme 2 and 3
29.8
carbobenzoxy-Gly-L-Trp
-
mixture of isoenzyme 2 and 3
73.4 - 90.5
carbobenzoxy-Gly-L-Trp
-
-
1.28
Carbobenzoxy-Gly-Leu
-
-
5.85
Carbobenzoxy-Gly-Phe
-
-
76.7
cinnamoyl-L-phenyllactate
-
-
0.015
Gly-L-Tyr
-
-
0.1
hippuryl-DL-beta-phenyllactate
-
pH 7.5, 25C, wild-type enzyme
0.39
hippuryl-DL-beta-phenyllactate
-
pH 7.5, 25C, mutant enzyme Y248F
635
hippuryl-DL-phenylacetic acid
-
-
-
0.081
hippuryl-DL-phenyllactate
-
-
0.88
hippuryl-L-Phe
-
pH 7.5, 25C, wild-type enzyme
4
hippuryl-L-Phe
-
pH 7.5, 25C, mutant enzyme Y248F
5.1
hippuryl-L-Phe
-
pH 7.5, 25C, mutant enzyme Y248A
6.08
hippuryl-L-Phe
-
pH 7.5, 25C, wild-type enzyme
17.7
hippuryl-L-Phe
-
-
40
hippuryl-L-Phe
-
-
4.3
hippuryl-L-phenylalanine
-
pH 7.4, 25C, recombinant enzyme
454
hippuryl-L-phenyllactate
-
-
933
hippuryl-L-phenyllactate
-
-
1000
hippuryl-L-phenyllactate
-
mixture of isoenzyme 2 and 3
5.98
hippuryl-Phe
-
-
81
hippuryl-Phe
-
pH 7.5
0.276
L-beta-phenyllactate-alpha-((2-naphthoyl)amino)-cinnamoyl ester
-
-
0.725
L-beta-phenyllactate-alpha-(acetylamino)-cinnamoyl ester
-
-
0.46
L-beta-phenyllactate-alpha-(benzoylylamino)-cinnamoyl ester
-
-
2.33
Leu-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
3.43
Met-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
1.45
Met-enkephalin-L-Arg-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.09
methotrexate-alpha-(1-naphthyl)alanine
-
pH 7.4, 25C, recombinant enzyme
667
N-(2-furanacryoyl)-Phe-Phe
-
-
-
7.6
N-(3-[2-furyl]acryloyl)-Phe-Phe
Q6ZXB9
in the absence of Co2+
11
N-(3-[2-furyl]acryloyl)-Phe-Phe
Q6ZXB9
in the presence of Co2+
86
N-acetyl-Gly-L-phenyllactic acid
-
-
14
N-carbobenzoxy-Gly-Gly-L-Leu
-
carboxypeptidase 2
199
N-carbobenzoxy-Gly-Gly-L-Leu
-
carboxypeptidase 1
57
N-carbobenzoxy-Gly-Gly-L-Phe
-
carboxypeptidase 1
97
N-carbobenzoxy-Gly-Gly-L-Phe
-
carboxypeptidase 2
16.8
N-carbobenzoxy-Gly-L-Phe
-
carboxypeptidase 2
22.4
N-carbobenzoxy-Gly-L-Phe
-
carboxypeptidase 1
14.4
N-carbobenzoxy-Gly-L-Tyr
-
carboxypeptidase 1
26.2
N-carbobenzoxy-Gly-L-Tyr
-
carboxypeptidase 2
0.05
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25C, wild-type enzyme
0.55
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25C, mutant enzyme Y248F
1
N-[3-(2-furyl)acryloyl]-Phe-Phe
-
pH 7.5, 25C, mutant enzyme Y248A
0.24
neurotensin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
0.11
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25C, wild-type enzyme
0.27
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25C, mutant enzyme Y248F
0.56
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25C, mutant enzyme Y248A
6.08
O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate
-
pH 7.5, 25C, mutant enzyme Y248A
0.042
p-nitrophenyl acetate
-
-
1.9
methotrexate-alpha-phenylalanine
-
pH 7.4, 25C, recombinant enzyme
additional information
additional information
-
comparison of turnover numbers of enzyme crystals and solution
-
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
65
3-(2-furyl)acryloyl-L-Phe-L-Ala
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
40116
532
3-(2-furyl)acryloyl-L-Phe-L-Ile
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
40114
693
3-(2-furyl)acryloyl-L-Phe-L-Leu
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
40113
581
3-(2-furyl)acryloyl-L-Phe-L-Met
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
40115
797
3-(2-furyl)acryloyl-L-Phe-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
40111
93
3-(2-furyl)acryloyl-L-Phe-L-Trp
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
40112
338
3-(2-furyl)acryloyl-L-Phe-L-Val
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
40117
36
angiotensin I
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
690
14
Leu-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
3082
6.2
Met-enkephalin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
2567
157
Met-enkephalin-L-Arg-L-Phe
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
40118
730
neurotensin
-
in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37C
2209
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
(+-)-2-benzylsuccinic acid
-
-
0.00001
(2E)-2-mercapto-3-phenylacrylic acid
-
pH 7.5, 25C
0.0021
(2E)-2-mercapto-4-phenylbut-2-enoic acid
-
pH 7.5, 25C
0.00135
(2E)-2-mercapto-5-phenylpent-2-enoic acid
-
pH 7.5, 25C
5.4
(2R,3S)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, substrate: hippuryl-L-Phe
5.7
(2R,3S)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, substrate: O-(trans-p-chlorocinnamyl)-L-beta-phenyllactate
0.3
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, mutant enzyme Y248F
0.34
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, substrate: hippuryl-L-Phe
0.35
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, wild-type enzyme
1.1
(2R,3S)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, mutant enzyme Y248A
2.79
(2R,4S)-2-benzyl-3-methanesulfinylpropanoic acid
-
pH 7.5
0.0000000048
(2S)-2-([hydroxy[(1R)-1-[[1-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-prolyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.00000018
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-b-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.0000000084
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.000000059
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-phenylalanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.000000082
(2S)-2-([hydroxy[(1R)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.000000077
(2S)-2-([hydroxy[(1S)-1-[[1-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-prolyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.0000009
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-b-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.00000009
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-alanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.0000021
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)-L-phenylalanyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.0000042
(2S)-2-([hydroxy[(1S)-1-[[N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl]amino]ethyl]phosphoryl]oxy)-3-phenylpropanoic acid
-
pH 7.5, 25C
0.0000009
(2S)-2-[(hydroxy[(1R)-1-[(1,4,7,10-tetraazacyclododecan-1-ylacetyl)amino]ethyl]phosphoryl)oxy]-3-phenylpropanoic acid
-
pH 7.5, 25C
1.1
(2S,3R)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, substrate: O-(trans-p-chlorocinnamyl)-L-beta-phenyllactate
2.2
(2S,3R)-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, substrate: hippuryl-L-Phe
0.19
(2S,3R)-2-benzyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, substrate: hippuryl-L-Phe
3.86
(2S,4R)-2-benzyl-3-methanesulfinylpropanoic acid
-
pH 7.5
0.56
(2S,4S)-2-benzyl-3-methanesulfinylpropanoic acid
-
pH 7.5
1.46
(R)-2-benzyl-3-(methylthio)propanoic acid
-
pH 7.5
1.4
(R)-2-benzyl-3-(N-sulfamoyl)aminopropanoic acid
-
pH 7.5
0.00015
(R)-2-benzyl-3-nitropropanoic acid
-
-
0.00043
(R)-2-benzyl-5-nitro-4-oxopentanoic acid
-
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.405
(R)-hippuryl-alpha-MePhe
-
pH 7.5
0.00036
(R)-N-(2-chloroethyl)-N-methylphenylalanine
-
pH 7.5
0.072
(R)-N-(N-hydroxysulfamoyl)phenylalanine
-
pH 7.5
0.033
(R)-N-benzylcysteine
-
pH 7.5, 25C
0.0079
(R)-N-cyclohexylcysteine
-
pH 7.5, 25C
0.00056
(R)-N-formyl-N-hydroxyphenylalanine
-
pH 7.5
0.039
(R)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
pH 7.5
0.0029
(R)-N-isopropylcysteine
-
pH 7.5, 25C
0.00061
(R)-N-phenethylcysteine
-
pH 7.5, 25C
0.47
(R)-N-sulfamoylphenylalanine
-
pH 7.5
0.031
(R,S)-2-benzyl-5-nitro-4-oxopentanoic acid
-
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
-
0.00209
(R,S)-N-(hydroxyaminocarbonyl)-phenylalanine
-
pH 7.5
0.1
(RS)-2-benzyl-3-(methylthio)propanoic acid
-
pH 7.5
0.00079
(RS)-2-benzyl-3-nitropropanoic acid
-
-
0.00353
(RS)-2-benzyl-3-sulfamoylpropionic acid
-
pH 7.5
0.002
(RS)-2-isobutyl-3-nitropropanoic acid
-
-
0.00038
(RS)-2-mercaptomethyl-2-methyl-3-phenylpropanoic acid
-
pH 7.5
0.00011
(RS)-2-mercaptomethyl-2-methylbutanoic acid
-
pH 7.5
0.0001
(RS)-2-mercaptomethylbutyric acid
-
pH 7.5
0.00198
(RS)-3-phenyl-2-sulfamoyloxypropionic acid
-
pH 7.5
0.00209
(RS)-N-(hydroxyaminocarbonyl)-phenylalanine
-
pH 7.5
0.067
(RS)-N-formyl-N-hydroxyphenylalanine
-
pH 7.5
0.00142
(RS)-N-sulfamoylphenylalanine
-
pH 7.5
0.000000015
(S)-2-(Hydroxy-[(S)-1-[(S)-3-methyl-2-(2-1,4,7,10tetraaza-cyclododec-1-yl-acetylamino)-pentanoylamino]-ethyl]-phosphinoyloxy)-3-phenyl-propionic acid
-
pH 7.5, 25C
0.00000026
(S)-2-(Hydroxy-[(S)-1-[(S)-3-methyl-2-(2-1,4,7,10tetraaza-cyclododec-1-yl-acetylamino)-pentanoylamino]-ethyl]-phosphinoyloxy)-3-phenyl-propionic acid
-
pH 7.5, 25C
0.74
(S)-2-benzyl-3-(methylthio)propanoic acid
-
pH 7.5
2.9
(S)-2-benzyl-3-(N-sulfamoyl)aminopropanoic acid
-
pH 7.5
0.068
(S)-2-benzyl-3-nitropropanoic acid
-
-
0.00016
(S)-2-benzyl-5-nitro-4-oxopentanoic acid
-
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.0025
(S)-N-(2-chloroethyl)-N-methylphenylalanine
-
pH 7.5
0.035
(S)-N-(N-benzylsulfamoyl)phenylalanine
-
pH 7.5
0.0032
(S)-N-(N-hydroxysulfamoyl)phenylalanine
-
pH 7.5
0.61
(S)-N-(N-isopropylsulfamoyl)phenylalanine
-
pH 7.5
0.18
(S)-N-(N-methylsulfamoiyl)phenylalanine
-
pH 7.5
0.18
(S)-N-(N-phenylethylsulfamoyl)phenylalanine
-
pH 7.5
0.00019
(S)-N-benzylcysteine
-
pH 7.5, 25C
0.0029
(S)-N-cyclohexylcysteine
-
pH 7.5, 25C
0.00495
(S)-N-formyl-N-hydroxyphenylalanine
-
pH 7.5
1.9
(S)-N-hydroxy-N-sulfamoyl-beta-phenylalanine
-
pH 7.5
0.00056
(S)-N-isopropylcysteine
-
pH 7.5, 25C
3.5
(S)-N-methyl-N-sulfamoylphenylalanine
-
pH 7.5
0.000055
(S)-N-phenethylcysteine
-
pH 7.5, 25C
0.00065
(S)-N-sulfamoylphenylalanine
-
pH 7.5
0.00065
(S)-N-sulfamoylphenylalanine benzyl ester
-
pH 7.5
0.00529
2-(1-hydroxy-5-oxopyrrolidin-2-yl)-3-phenylpropanoic acid
-
25C, limiting value for Ki-value at intermediate pH
0.000011
2-benzyl-3-mecaptopropionate
-
-
0.00015
2-benzyl-3-nitropropanoic acid
-
-
0.00259
2-benzyl-3-[(difluoroacetyl)(hydroxy)amino]propanoic acid
-
25C, limiting value for Ki-value at intermediate pH
0.012
2-benzyl-3-[(fluoroacetyl)(hydroxy)amino]propanoic acid
-
25C, limiting value for Ki-value at intermediate pH
0.00139
2-benzyl-3-[formyl(hydroxy)amino]propanoic acid
-
25C, limiting value for Ki-value at intermediate pH
0.009
2-benzyl-3-[hydroxy(methoxyacetyl)amino]propanoic acid
-
25C, limiting value for Ki-value at intermediate pH
0.0994
2-benzyl-3-[hydroxy(methoxycarbonyl)amino]propanoic acid
-
25C, limiting value for Ki-value at intermediate pH
0.00942
2-benzyl-3-[hydroxy(trifluoroacetyl)amino]propanoic acid
-
25C, limiting value for Ki-value at intermediate pH
0.207
2-benzyl-4-oxopentanoic acid
-
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.0002
2-benzyl-5,5,5-trifluoro-4-oxopentanoic acid
-
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.015
2-benzyl-5-bromo-4-oxopentanoic acid
-
in 0.05 M Tris/0.5 M NaCl buffer, pH 7.5
0.0242
3-hydroxyaminocarbonyl-2-benzylpropanoic acid
-
pH 7.5, 25C
0.062
3-Phenylpropionic acid
-
-
0.482
3-Phenylpropionic acid
-
-
6.1
3-Phenylpropionic acid
-
-
0.00806
3-[acetyl(hydroxy)amino]-2-benzylpropanoic acid
-
25C, limiting value for Ki-value at intermediate pH
0.118
4-Phenylbutyric acid
-
-
0.039
aminobenzylsuccinic acid
-
-
-
0.0055
anilino(mercapto)acetic acid
-
-
0.0000239
Ascaris carboxypeptidase inhibitor
-
-
-
0.00000071
CBZ-Ala-Gly-PSI[P(O2)O]-Phe
-
crystallographic study of structure
5
cinnamate
-
-
0.0023
D-Cys
-
zinc carboxypeptidase A
0.0023
D-Cys
-
pH 7.5, 25C
20
D-His
-
-
0.00154
D-N-(hydroxyaminocarbonyl)phenylalanine
-
pH 7.5, 25C
0.0015
D-N-hydroxyaminocarbonyl phenylalanine
-
-
1.2
D-penicillamine
-
zinc carboxypeptidase A
0.074
D-Phe
-
-
2
D-Phe
-
-
0.014
D-Trp
-
-
0.1
Gly-L-Tyr
-
-
0.078
indole acetic acid
-
-
0.35
L-Cys
-
zinc carboxypeptidase A
0.35
L-Cys
-
pH 7.5, 25C
0.01898
L-N-(aminocarbonyl)phenylalanine
-
pH 7.5, 25C
0.00456
L-N-(hydroxyaminocarbonyl)phenylalanine
-
pH 7.5, 25C
0.0046
L-N-hydroxyaminocarbonyl phenylalanine
-
-
1.7
L-Penicillamine
-
zinc carboxypeptidase A
0.0021
L-Phe-phosphoramidate-phenylester
-
-
0.058
L-Phenyllactate
-
-
0.000003
latexin
-
pH 7.5, recombinant CPA4
-
0.000003
latexin
-
-
-
0.0000073
leech carboxypeptidase inhibitor
-
-
-
0.0024
mercapto(methylamino)acetic acid
-
pH 7.5, 25C
0.000000026
N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl-N-[(1R)-1-[[(1S)-1-carboxy-2-phenylethoxy](hydroxy)phosphoryl]ethyl]glycinamide
-
pH 7.5, 25C
0.0000032
N-(1,4,7,10-tetraazacyclododecan-1-ylacetyl)glycyl-N-[(1S)-1-[[(1S)-1-carboxy-2-phenylethoxy](hydroxy)phosphoryl]ethyl]glycinamide
-
pH 7.5, 25C
0.0021
N-phenylphosphoryl-L-phenylalanine
-
-
2.5
p-Nitrophenylacetic acid
-
-
0.001
Phe phosphonate
-
-
0.39
phenylacetic acid
-
-
0.000001
polypeptide inhibitor
-
molecular weight 10000
-
0.0000013
Potato carboxypeptidase inhibitor
-
-
-
0.0000017
Potato carboxypeptidase inhibitor
-
-
-
0.000002
Potato carboxypeptidase inhibitor
-
-
-
0.000005
Potato carboxypeptidase inhibitor
-
-
-
0.000107
Potato carboxypeptidase inhibitor
-
-
-
0.0000069
potato carboxypeptidase inhibitor mutant DELTA39
-
-
-
0.0000185
potato carboxypeptidase inhibitor mutant F23A
-
pH 7.5
-
0.00044
potato carboxypeptidase inhibitor mutant F23A/W28A
-
pH 7.5
-
0.0000023
potato carboxypeptidase inhibitor mutant H15A
-
pH 7.5
-
0.0000015
potato carboxypeptidase inhibitor mutant N29A
-
pH 7.5
-
0.0000019
potato carboxypeptidase inhibitor mutant N29A/S30A
-
pH 7.5
-
0.0000035
potato carboxypeptidase inhibitor mutant N29G
-
pH 7.5
-
0.000125
potato carboxypeptidase inhibitor mutant P36G
-
-
-
0.0000014
potato carboxypeptidase inhibitor mutant S30A
-
pH 7.5
-
0.0000079
potato carboxypeptidase inhibitor mutant W22A
-
pH 7.5
-
0.0000132
potato carboxypeptidase inhibitor mutant W28A
-
pH 7.5
-
0.0000056
potato carboxypeptidase inhibitor mutant Y37G
-
-
-
0.000347
potato carboxypeptidase inhibitor mutant Y37G/DELTA39
-
-
-
0.00235
rac-2-(mercaptomethyl)-3-cyclohexylpropanoic acid
-
pH 7.5, 25C
0.00016
rac-2-(mercaptomethyl)-4-methylpentanoic acid
-
pH 7.5, 25C
0.000011
rac-2-benzyl-3-mercaptopropanoic acid
-
pH 7.5, pH 25C
0.0016
rac-2-benzyl-5-chloropentanoic acid
-
pH 7.5
0.00081
rac-N-(1-naphthylmethyl)cysteine
-
pH 7.5, 25C
0.0585
rac-N-(aminocarbonyl)phenylalanine
-
pH 7.5, 25C
0.0094
rac-N-(cyclohexylmethyl)cysteine
-
pH 7.5, 25C
0.00209
rac-N-(hydroxyaminocarbonyl)phenylalanine
-
pH 7.5, 25C
0.00085
rac-N-(p-methoxy)benzylcysteine
-
pH 7.5, 25C
0.012
rac-N-benzyl-N-methylcysteine
-
pH 7.5, 25C
0.00027
rac-N-benzylcysteine
-
pH 7.5, 25C
0.0096
rac-N-cyclohexylcysteine
-
pH 7.5, 25C
0.0014
rac-N-ethylcysteine
-
pH 7.5, 25C
0.0075
rac-N-isobutylcysteine
-
pH 7.5, 25C
0.0011
rac-N-isopropylcysteine
-
pH 7.5, 25C
0.000065
rac-N-phenethylcysteine
-
pH 7.5, 25C
0.0013
rac-N-phenylpropylcysteine
-
pH 7.5, 25C
0.0056
rac-N-propylcysteine
-
pH 7.5, 25C
0.0013
rac2-(mercaptomethyl)-6-phenylhexanoic acid
-
pH 7.5, 25C
5.9
threo-2-benzyl-2-methyl-3,4-epoxybutanoic acid
-
pH 7.5, 25C, substrate: hippuryl-L-Phe
0.0000008
tick carboxypeptidase inhibitor
-
-
-
0.0000016
wild-type potato carboxypeptidase inhibitor
-
pH 7.5
-
0.00022
mercaptoacetyl-D-Phe
-
-
additional information
additional information
-
D-penicillamine sulfide: Ki-value above 27 mM
-
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
-
residual enzyme activity, 0.2% chitosan hydrochloride 55% activity, 0.2% chitosan citrate 0% activity, 0.04% 8% activity, 0.02% 15% activity, 0.01% 65% activity
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
Gly-Asn-Arg-Pro-Thr
Q9UI42
-
0.72
Phe-Asn-Arg-Ala-Val-Asp
Q9UI42
-
0.63
Phe-Asn-Arg-Ala-Val-Val
Q9UI42
-
4
Phe-Asn-Arg-Pro-Val
Q9UI42
-
5
Phe-Asn-Arg-Pro-Val
Q9UI42
IC50 4-6 mM
0.91
Phe-Asn-Arg-Pro-Val-Asp
Q9UI42
-
0.71
Phe-Asn-Arg-Pro-Val-Val
Q9UI42
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0064
-
gut extract
0.09
-
carboxypeptidase A, pH 5.6
2.8
-
Aspergillus niger extract, pH 5.6; carboxypeptidase A, pH 7.5
7.2
-
purified recombinant enzyme, substrate hippuryl-L-phenylalanine
9.2
-
Aspergillus niger extract, pH 8.5
10.8
-
carboxypeptidase A, pH 8.5
11.7
-
recombinant enzyme secreted from Pichia pastoris, cell-free supernatant
14.4
-
culture filtrate
33.5
-
Aspergillus niger extract, pH 7.5; purification step acetone precipitation
35.8
-
purification step Macro-Prep High Q
59.8
-
-
108
-
-
850
-
purified recombinant enzyme, substrate hippuryl-L-phenyllactate
additional information
-
-
additional information
-
activity in fresh serum, liver, heart tissues
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
comparison of activities of enzyme immobilized on different supports, highest activity for polyacrylamide bead support
additional information
-
mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A
additional information
-
catalytic efficency of the purified recombinant enzyme
additional information
-
in vivo enzyme activity in presence and absence of Cd2+
additional information
-
activity in gut sections
additional information
-
modulation of the secretin-caerulin-test for determnination of enzyme as well as zinc exocrine out of the pancreas, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
esterase activity, broad optimum
6.5
-
activity assay, suboptimal condition because chitosan is soluble only until pH 6-6.5
7 - 8
-
substrate-dependent
7 - 8.5
-
-
7 - 8.5
-
esterase activity, broad optimum
7 - 9
-
-
7 - 9
-
-
7.4 - 7.8
-
buffer-dependent, Tris better than phosphate buffer
7.4
-
assay at
7.5 - 8
-
-
7.5 - 8
-
-
7.5 - 8
-
identical for soluble and immobilized enzymes
7.5
-
-
7.5
-
assay at
7.5
-
assay at
7.5
-
assay at
7.5
-
assay at
7.5
-
buffer-dependent
7.5
-
assay at
7.5
-
activity assay
7.5
-
activity assay
7.6
Q6ZXB9
-
8 - 8.5
-
-
8 - 8.5
-
-
8
-
peptidase activity, sharp optimum
8
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
carboxypeptidase activity assay; carboxypeptidase activity assay; carboxypeptidase activity assay; carboxypeptidase activity assay; carboxypeptidase activity assay; carboxypeptidase activity assay
8
Q9UI42
activity assay
8
-
hydrolysis of protein isolates of Brassica carinata in a batch reactor, trypsin, chymotrypsin, and carboxypeptidase A are used
8.5
-
assay at
8.5
Cephalopina titillator
-
-
additional information
-
pK-values of active residues
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 4.9
-
-
5 - 10
-
pH 5: about 20% of maximum activity, pH 10: about 50% of maximum activity
5 - 9
-
-
5.5 - 10
-
pH 5.5: about 35% of maximum activity, pH 10: about 40% of maximum activity
6 - 9.5
-
pH 6.0, pH 9.5: about 25% of maximum peptidase activity
6 - 9.5
-
pH 6.0: about 25% of maximum activity, pH 9.5: about 70% of maximum activity
7 - 8
-
-
7.6 - 8
Q6ZXB9
-
8.5 - 9
-
the optimal pH for cleavage of 3-(2-furyl)acryloyl-L-Phe-L-Phe and 3-(2-furyl)acryloyl-L-Phe-L-Ala is in the range of 8.5-9.0 with very low activity below pH 6.0
additional information
-
effects of pH on structure and catalytic properties
additional information
-
pK values of active site residues
additional information
-
pH-dependent properties of cobalt enzymeinhibitor complexes
additional information
-
effect of pH on zinc inhibition
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
no measurements below
20
-
assay at
21
-
assay at
22
-
activity assay at room temperature
24
-
activity assay
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
25
-
kinetic assay
30 - 35
-
soluble enzyme
30
-
assay at
30
-
assay at
30
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
carboxypeptidase activity assay; carboxypeptidase activity assay; carboxypeptidase activity assay; carboxypeptidase activity assay; carboxypeptidase activity assay; carboxypeptidase activity assay
37
-
assay at
37
-
assay at
37
-
assay at
37
-
activity assay
37
-
activity assay
50 - 55
-
immobilized enzyme
50
-
hydrolysis of protein isolates of Brassica carinata in a batch reactor, trypsin, chymotrypsin, and carboxypeptidase A are used
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
30C, native enzyme: about 60% of maximum activity, immobilized enzyme: about 65% of maximum activity, 70C, native enzyme: about 10% of maximum activity, immobilized enzyme: about 80% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.08
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
predicted pI value, clone ID AM1-02, carboxypeptidase A; predicted pI value, clone ID AM1-30, carboxypeptidase A homolog; predicted pI value, clone ID AM3-75, carboxypeptidase A; predicted pI value, clone ID L4-60, carboxypeptidase A
5.15
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
theoretical pI value MDCP-A1b; theoretical pI value MDCP-A1c
5.22
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
theoretical pI value MDCP-A1a; theoretical pI value MDCP-A1e
5.29
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
theoretical pI value MDCP-A1d
5.3
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
predicted pI value, clone ID AM1-72, carboxypeptidase A homolog; predicted pI value, clone ID AM2-60, carboxypeptidase A
6.2
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
predicted pI value, clone ID AM2-51, carboxypeptidase A
6.2
-
calculated from amino acid sequence
6.46
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
theoretical pI value MDCP-A2
8.75
Q8AXN4
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
granulated mast cell derived from undifferentiated mast cells by treatment with hematopoietic cytokines
Manually annotated by BRENDA team
-
granulated mast cell derived from undifferentiated mast cells by treatment with hematopoietic cytokines
Manually annotated by BRENDA team
-
mainly, protein P30, tentatively identified as inactive monomeric carboxypeptidase based on immunoreaction, properties shared with tubulin carboxypeptidase A
Manually annotated by BRENDA team
-
broadly distributed
Manually annotated by BRENDA team
Mus musculus C57B6
-
broadly distributed
-
Manually annotated by BRENDA team
Mus musculus C57B6
-
-
-
Manually annotated by BRENDA team
-
mast cell
Manually annotated by BRENDA team
Q5U901
low CPA6 expression level
Manually annotated by BRENDA team
Q60F93
during molting periods
Manually annotated by BRENDA team
Mus musculus C57B6
-
-
-
Manually annotated by BRENDA team
-
evenly distributed activity in the anterior and middle sections, but almost no activity in the posterior section
Manually annotated by BRENDA team
Q5U901
low expression levels in cingulate cortex, lateral septum, pontine nucleus, and inferior olivary nucleus
Manually annotated by BRENDA team
P15088
low expression level
Manually annotated by BRENDA team
-
integument from the 5th instar larvae
Manually annotated by BRENDA team
-
integument of insect at molting, prepupal and pupal ecdysis stages
Manually annotated by BRENDA team
P15088
low expression level
Manually annotated by BRENDA team
-
third larval instar
Manually annotated by BRENDA team
P15088
high expression level, high expression level, dispersed lung cells enriched for mast cells
Manually annotated by BRENDA team
-
the cDNA of hCPA is obtained by RT-PCR from lung tissues
Manually annotated by BRENDA team
-
in primary macrophages, CPVL is glycosylated with high mannose residues
Manually annotated by BRENDA team
-
from bone marrow, undifferentiated
Manually annotated by BRENDA team
-
peritoneal, cathepsin B or E deficient
Manually annotated by BRENDA team
-
peritoneal, MCCPA localization analysis
Manually annotated by BRENDA team
-
mucosal mast cell
Manually annotated by BRENDA team
-
the expression of human MC-CPA seems to be restricted to the MCTC subclass
Manually annotated by BRENDA team
Cephalopina titillator
-
-
Manually annotated by BRENDA team
-
of the third larval instar
Manually annotated by BRENDA team
-
molting fluid in the molting- and prepupal-stage larvae
Manually annotated by BRENDA team
-
molting fluid of insect at molting, prepupal and pupal ecdysis stages
Manually annotated by BRENDA team
-
vaginal mucosa
Manually annotated by BRENDA team
Q5U901
high CPA6 expression level, enriched in the mitral and granular layers
Manually annotated by BRENDA team
Mus musculus C57B6
-
-
-
Manually annotated by BRENDA team
-
elaborated as inactive proenzyme by acinar cells
Manually annotated by BRENDA team
-
activated pancreatic juice
Manually annotated by BRENDA team
-
activated pancreatic juice
Manually annotated by BRENDA team
-
duct cell of the pancreas, pancreatic ductal epithelial cell
Manually annotated by BRENDA team
-
luminally secreted protease
Manually annotated by BRENDA team
-
PC-3m human prostate cancer cell line
Manually annotated by BRENDA team
P15088
low expression level
Manually annotated by BRENDA team
Q5U901
low CPA6 expression level
Manually annotated by BRENDA team
-
antigen A33-prositive colon carcinoma cell line
Manually annotated by BRENDA team
Mus musculus C57B6
-
abundant
-
Manually annotated by BRENDA team
-
expressed in phorbol myristate acetate-stimulated cells
Manually annotated by BRENDA team
Q60F93
the enzyme expression is induced during pupal ecdysis
Manually annotated by BRENDA team
-
CPVL is up-regulated during the maturation of monocytes to macrophages. Expression in monocyte-derived dendritic cells
Manually annotated by BRENDA team
additional information
Q60F93
expression analysis during pupal ecdysis, overview
Manually annotated by BRENDA team
additional information
P15088
MC-CPA expression analysis, overview
Manually annotated by BRENDA team
additional information
Q5U901
tissue distribution of carboxypeptidase A-6, in situ hybridization, overview
Manually annotated by BRENDA team
additional information
-
present in Jurkat T-cell line, is not expressed by monocyte depleted peripheral blood mononuclear cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Phaffia rhodozyma CBS 5905
-
-
-
-
Manually annotated by BRENDA team
Mus musculus C57B6
-
-
-
Manually annotated by BRENDA team
Q60F93
molting fluid
-
Manually annotated by BRENDA team
-
CPVL present in early (5 min incubation) latex bead phagosomes, it is not retained in the mature, cathepsin D-positive phagolysosome (60 min incubation)
-
Manually annotated by BRENDA team
-
MCCPA- and histamine-containing secretory granules from mast cells
Manually annotated by BRENDA team
-
MC-CPA is a dominant protein component of the mast cell granule
Manually annotated by BRENDA team
-
present in ruffles of macrophages, absent from outer plasma membrane
Manually annotated by BRENDA team
additional information
-
MCCPA subcellular localization, overview
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28900
-
gel filtration
36338
30000
-
boundary depletion sedimentation equilibrium
36330
33520
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
predicted molecular mass, clone ID AM2-51, carboxypeptidase A
683542
34000
-
gel filtration
36331
34370
-
amino acid analysis
36319
34400
-
SDS-PAGE, type beta
36360
34490
-
amino acid sequence
36322
34600
-
SDS-PAGE, type gamma
36360
34650
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
predicted molecular mass, clone ID AM1-02, carboxypeptidase A
683542
34800
-
sedimentation equilibrium
36335
34860
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
predicted molecular mass, clone ID AM1-72, carboxypeptidase A homolog
683542
34870
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
predicted molecular mass, clone ID AM2-60, carboxypeptidase A
683542
34900
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
predicted molecular mass, clone ID AM1-30, carboxypeptidase A homolog
683542
34990
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
predicted molecular mass, clone ID AM3-75, carboxypeptidase A; predicted molecular mass, clone ID L4-60, carboxypeptidase A
683542
35000
-
in presence of urea and 2-mercaptoethanol, SDS-PAGE
36325
35000
-
gel filtration
36329
35000
-
sedimentation equilibrium
36334
35470
-
alpha form, amino acid analysis
36317
35780
-
mature enzyme after cleavage of the signal- and activation peptides
706874
36000
-
fully processed form of MC-CPA, SDS-PAGE
706874
37800
-
SDS-PAGE, component II
36324
38000
-
native ASPA expessed in COS-7 cells, determined by immunoblotting
678979
38900
-
gel filtration
36338
39300
-
SDS-PAGE, component I
36324
40000
-
gel filtration
36326
42000
-
determined by SDS-PAGE and Western blotting
681146
47570
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
theoretical molecular mass MDCP-A2
668948
47790
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
theoretical molecular mass MDCP-A1d
668948
47820
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
theoretical molecular mass MDCP-A1a
668948
47850
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
theoretical molecular mass MDCP-A1e
668948
47890
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
theoretical molecular mass MDCP-A1b; theoretical molecular mass MDCP-A1c
668948
48730
-
calculated from amino acid sequence
706874
52000
-
recombinant human ASPA fused to N-terminal thioredoxin and C-terimal V5 and a 6x-histidine tag, analyzed by SDS-PAGE
678979
53600
-
calculated from amino acid sequence
704029
54000
-
SDS-PAGE
704029
105700
-
biotin-PEG(5000)-carboxypeptidase complex, stoichiometry with avidin 1 : 1, determined by MALDI-TOF
683198
130000
-
Western blot analysis
686638
132000
Q6ZXB9
gel filtration
684959
142300
-
biotin-PEG(3400)-carboxypeptidase complex, stoichiometry with avidin 1 : 2, determined by MALDI-TOF
683198
146300
-
biotin-PEG(3400)-carboxypeptidase-PEG(2000) complex, stoichiometry with avidin 1 : 2, determined by MALDI-TOF
683198
233000
-
biotin-PEG(5000)-carboxypeptidase-PEG(2000) complex, stoichiometry with avidin 1 : 4, determined by MALDI-TOF
683198
additional information
-
molecular weight of trimeric procarboxypeptidase 87000, molecular weight of carboxypeptidase precursor subunit 40000-42000, slight differences in molecular weight may be caused by different activation conditions
36317
additional information
-
molecular weight of dimeric procarboxypeptidase 72500; molecular weight of trimeric procarboxypeptidase 87000, molecular weight of carboxypeptidase precursor subunit 40000-42000, slight differences in molecular weight may be caused by different activation conditions
36322
additional information
-
enzyme-inhibitor complex
670750
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 36000
?
-
x * 47140, prepro-CPA1, sequence calculation, x * 34000, recombinant mature CPA1, SDS-PAGE, x * 42000, recombinant proCPA1, SDS-PAGE
?
-
x * 80000, recombinant fusion enzyme expressed in Escherichia coli, SDS-PAGE, x * 36000, recombinant detagged enzyme expressed in Escherichia coli, SDS-PAGE, x * 37000, recombinant enzyme expressed in Pichia pastoris, SDS-PAGE
?
Q6ZXB9
x * 58300, sequence analysis, x * 58000, polyclonal anti-MCP-2 peptide serum
monomer
-
-
monomer
-
1 * 40000, SDS-PAGE
monomer
-
SDS-PAGE
monomer
-
SDS-PAGE
monomer
-
in solution, crystallography
additional information
-
-
additional information
-
structure of enzyme and its complex with substrate, overall conformation of the protein, analysis of secondary structures, structure of active center and zinc ligand complex
additional information
-
model of three-dimensional structure
additional information
-
tendency towards aggregation
additional information
-
amino terminal amino acid sequence analysis
additional information
-
proenzyme exists as aggregates of 2-3 subunits
additional information
-
amino acid composition described
additional information
-
amino acid composition described
additional information
-
amino acid composition described
additional information
-
amino acid composition described
additional information
-
amino acid composition described
additional information
-
structure analysis of enzyme in complex with leech carboxypeptidase inhibitor
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
Q60F93
the enzyme is secreted as zymogen and processed in the molting fluid
proteolytic modification
-
the proCPA1 is activated by cleavage by trypsin, the mature enzyme shows 115fold higher activity than the pro-enzyme
proteolytic modification
-
cleavage of the signal peptide and subsequent cleavage of the propeptide results in the formation of the mature enyzme
glycoprotein
-
-
proteolytic modification
-
the mast cell CPA is activated by proteolytic cleavage of the pro-enzyme by cathepsins B, L, D, and E, overview
proteolytic modification
-
cleavage of the signal peptide and subsequent cleavage of the propeptide results in the formation of the mature enyzme
proteolytic modification
Q8AXN4
the proCPA1 is activated by proteoltyic cleavage
proteolytic modification
-
cleavage of the signal peptide and subsequent cleavage of the propeptide results in the formation of the mature enzyme
proteolytic modification
-
the enzyme is produced as secreted pro-enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.25 A resolution
-
analysis of enzyme-substrate complex by difference Fourier techniques, analysis of enzyme-inhibitor complexes, mechanistic model based on crystal structure
-
comparison of three carboxypeptidase A-phosphonate complexes
-
complex of enzyme with the inhibitor (S)-N-sulfamoylphenylalaninecrystals are grown by the microdialysis method by equilibrating the protein-inhibitor complex in a solution of 1.2 M LiCl and 20 mM Tris-HCl buffer (pH 7.5) against a reservoir containing 0.2 M LiCl and 20 mM Tris-HCl buffer (pH 7.5)
-
crystal structure analysis
-
crystal structure of carboxypeptidase A complexed with D-cysteine at 1.75 A
-
crystal structure of complex with inactivator 2-benzyl-3-iodo-propanoic acid in two crystal forms
-
crystallization reduces catalytic efficiency, abolishes substrate inhibition observed in solution
-
enzyme in complex with leech carboxypeptidase inhibitor, complexing in 50 mM Tris-HCl, pH 7.5, and 100 mM NaCl, at 20C, complex purification by gel filtration, crystallization by mixing of equal volumes of protein, containing 10-12 mg/ml protein, and reservoir solutions, the latter containing 1.5 M lithium sulfate monohydrate and 100 mM Tris, pH 8.5, sitting drop vapour diffusion method, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
enzyme inhibitor complexes with D-N-hydroxyaminocarbonyl phenylalanine, L-N-hydroxyaminocarbonyl phenylalanine or aminocarbonylphenylalanine
-
high-resolution crystallographic studies of enzyme-substrate and enzyme-inhibitor complexes
-
mechanical deformation enhances catalytic activity of crystalline carboxypeptidase A
-
purified enzyme in complex with the tick carboxypeptidase inhibitor, X-ray diffraction structure determination and analysis at 1.7 A resolution, comparison to the structure of unligated enzyme PDB code 1M4L, overview
-
relationships between enzyme structure and catalytic properties
-
structural analysis of enzyme-GlyTyr complexes, design of mechanism-based inactivators based thereon
-
study of pH-structure relationships
-
x-ray absorption fine study of active site in solution and crystalline forms
-
at 1.7 A resolution, structure is organized into a four-layer alphabetabetaalpha topology, zinc ion residing between the central beta-sheets is partially coordinated by three histidine residues
-
CPA4-hexapeptide complex crystallized by sitting drop vapor diffusion method, to 1.6 A resolution; structural details of a true cleaved double-product complex with a hexapeptide of human ocarboxypeptidase A4 employing diffraction data to 1.6 A resolution are provided
Q9UI42
in complex with 2-benzyl-3,4-epithiobutanoic acid, hanging drop vapor diffusion method, using 20% PEG (w/v) 3350, 0.2 M NH4Cl, 0.02 M Tris pH 7.0
-
purified recombinant CPA4 in complex with latexin, hanging drop vapour diffusion method, 0.001 ml of 7 mg/ml protein solution is mixed with 0.001 ml reservoir solution containing 40% 2-methyl-2,4-pentanediol, 0.1 M [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)methane, pH 6.5, and with 0.002 ml 40% acetone, 20C, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 11.6
-
35% activity remaining at pH 4 after 30 min, 87% at pH 11.6
36335
5 - 9
-
at 25C
36338
6 - 9
-
-
36324
6
-
stable at or above, unstable below
36330
7 - 10
-
at 0C
36322
8.5
-
quick inactivation of soluble enzyme, no inactivation of immobilized enzyme
36354
additional information
-
-
36322
additional information
-
completely inactive at pH 5
36329
additional information
-
no major structural changes over pH range 7.5-9.5
36339
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
10 min, 50% loss of activity
36324
40
-
below
36338
40
-
below
36360
50
-
10 min, 50% loss of activity
36324
50
-
50 min, 90% loss of activity
36329
50
-
different stability in the 5 molecular species
36333
50
-
half-life: native enzyme 20 min, immobilized enzyme 2 h 48 min
36351
55
-
35% activity after 30 min of immobilized enzyme, no activity of soluble enzyme
36354
60
-
48% inactivation after 5 min
36335
60
-
half-life of purified recombinant CPA2 is 24 min, and 8fold longer than for CPA1
667298
additional information
-
-
36322
additional information
Q6ZXB9
residual activity after 5 min of incubation at 50C is 27.5%, the enzyme is not thermostable
684959
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
hydrophobic environment of immobilized enzyme enhances conformational stability
-
urea influences general stability, 4 M, 0C, pH 7.5, 24 h, stable, 7 M, 0C, pH 7.5, 24 h, unstable
-
immobilization on acid chloride or oxidised cellulose increases half-life from 20 min to 168 min
-
effect of ionic strength: marked decrease of activity above 150 mM NaCl
-
no effect of freezing and thawing
-
generally unstable at all stages of purification
-
freezing destabilizes, unstable in 0.72 M (NH4)2SO4, stable in 2.1 M (NH4)2SO4
-
little effect of urea on enzyme activity
-
unstable upon lyophilization
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, lyophilized powder, indefinite, proenzyme
-
0.1 mg/ml bovine serum albumin and Zn2+ stabilize the washed enzyme crystals from a commercial preparation
-
0C, Tris-HCl, pH 7.5, crystals under toluene atmosphere, indefinite
-
4C, Tris-HCl, pH 8.0, 0.1 M NaCl
-
4C, immobilized enzyme, 6 months, 8% loss of activity
-
-20C, NaCl-HEPES, pH 7.5, purified enzyme, 1 month, 10% loss of activity
-
0C, sodium phosphate, pH 5.8, 17% saturation ammonium phosphate, toluene, crystals
-
4C, ammonium sulfate, pH 6.0, precipitated procarboxypeptidase
-
5C, Tris-HCl, pH 7.5, crystals under toluene atmosphere, indefinite
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the enzyme is purified from the culture medium by acetone precipitation and Macro-Prep High Q anion exchange chromatography
-
also brain protein P30
-
also procarboxypeptidase
-
from pancreatin
-
further purification of commercial preparation by gel filtration in presence of Zn2+ and latexin
-
the biotin-PEGylated carboxypeptidase complex is purified by gel filtration
-
using a CABS-sepharose affinity column
-
recombinant enzyme is purified by His-Bind resin column chromatography, endogenous enzyme is purified by CNBr-activated Sepharose column chromatography
-
by anion-exchange chromatography; the active protein is obtained through tryptic activation, the resulting protein-product complex is subsequently purified by anion-exchange chromatography
Q9UI42
by gel filtration and on anion-exchange column
-
purified with GST affinity chromatography
-
recombinant maltose binding protein-fusion enzyme from Escherichia coli by amylose affinity chromatography, digestion with thrombin, and heparin affinity chromatography
-
recombinant pro-CPA1 from Saccharomyces cerevisiae by anion exchange and hydrophobic interaction chromatography and another step of anion exchange chromatography followed by dialsis and gel filtration, to homogeneity
-
to more than 80% purity
-
TSK DEAE 5PW column chromatography
-
using nickel affinity chromatography
-
proteins were extracted from larvae and pupae of the insect, and adult flies; proteins were extracted from larvae and pupae of the insect, and adult flies; proteins were extracted from larvae and pupae of the insect, and adult flies; proteins were extracted from larvae and pupae of the insect, and adult flies; proteins were extracted from larvae and pupae of the insect, and adult flies; proteins were extracted from larvae and pupae of the insect, and adult flies
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
purified in one step using Co-NTA resin
Q6ZXB9
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene MF-CPA, phylogenetic analysis of the molting fluid carboxypeptidase A, expression analysis during development
Q60F93
expression in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) cells
-
a gamma-SmscFv/hCPA fusion protein is constructed, the pGEX-4T-1 and pUC19 vectors are used, recombinant proteins are expressed in Escherichia coli DH5alpha cells
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli as maltose binding protein-fusion protein with low activity level, methanol-inducible expression in Pichia pastoris with a high activity of the secreted recombinant enzyme
-
DNA and amino acid sequence determination and analysis, expression of the pro-CPA1 in Saccharomyces cerevisiae
-
DNA and amino acid sequence determination and analysis, the gene contains 11 exons and is located on chromosome 3, genetic organization, phylogenetic analysis
P15088
expressed in Pichia pastoris
-
expression of CPA4 in Pichia pastoris, scecretion of the recombinant enzyme to the culture medium
-
full-length human ASPA cDNA is subcloned into the pcDNA3.1/V5-His-TOPO vector, for bacterial expression mutants are generated directly in the pBAD/Thio-TOPO vector
-
hCPA4 is produced as a zymogen through recombinant heterologous overexpression using vector pPIC9 and the methylotrophic yeast Pichia pastoris; produced as a zymogen through recombinant heterologous overexpression using vector pPIC9 and the methylotrophic yeast Pichia pastoris as expression host
Q9UI42
into vector pET-28a(+) and expressed in Escherichia coli BL21-DE3 cells. BALB/c mice inoculated subcutaneously with recombinant CPVL. CHO cells transiently transfected with CPVL-EGFP expression vector
-
into vector pQTEV and introduced into Escherichia coli SCS1 cells carrying pRARE. The resulting clone used for expression of unlabeled protein. For expression of selenomethionine-labeled protein, the plasmid used to transform B834 Escherichia coli cells
-
subcloned into pcDNA3 lacking the KpnI site. MYPYDVPDYA ligated into the KpnI site of CCP1, which is located in the C-terminal region following the carboxypeptidase domain. Expression in Neuro2A and NIH3T3 cells
-
a cDNA library is constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into plasmid pCR2.1-TOPO; a cDNA library is constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into plasmid pCR2.1-TOPO; a cDNA library is constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into plasmid pCR2.1-TOPO; a cDNA library is constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into plasmid pCR2.1-TOPO; a cDNA library is constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into plasmid pCR2.1-TOPO; a cDNA library is constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into plasmid pCR2.1-TOPO
Q0QWG2, Q0QWG3, Q0QWG4, Q0QWG5, Q0QWG6, Q0QWG7
a pBSK-based vector construct is used for gene targeting
-
expression of His-tagged pro-enzyme in Escherichia coli and in HEK293 cells also expressing the Epstein Barr virus nuclear antigen 1, induction by A23187
-
gene Cpa6, DNA and amino acid sequence determination and analysis
Q5U901
DNA and amino acid sequence determination and analysis of the preproenzyme, phylogenetic analysis
Q8AXN4
comparison of exon sequence composition of different carboxypeptidases
-
four cDNA libraries are constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into a plasmid using a TOPO TA cloning kit; four cDNA libraries are constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into a plasmid using a TOPO TA cloning kit; four cDNA libraries are constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into a plasmid using a TOPO TA cloning kit; four cDNA libraries are constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into a plasmid using a TOPO TA cloning kit; four cDNA libraries are constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into a plasmid using a TOPO TA cloning kit; four cDNA libraries are constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into a plasmid using a TOPO TA cloning kit; four cDNA libraries are constructed using the SMART cDNA construction kit, the PCR fragments are cloned directly into a plasmid using a TOPO TA cloning kit
A1XG97, A1XG98, A1XG99, A1XGA0, A1XGA1, A1XGA2, A1XGA3
DNA and amino acid sequence determination and analysis of midgut carboxypeptidase A
-
expressed in Escherichia coli XL1 Blue cells as catalytically active poly-His-tagged recombinant enzyme. GST-fusion proteins expressed in Escherichia coli BL21 Codon Plus (DE3) cells
Q6ZXB9
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of CPA can be up-regulated by 20-hydroxyecdysone. In the integument, the transcription level of the gene reaches its peak at the 5th instar molting stage and the 6th instar prepupal stage, respectively
-
CPA4 is upregulated by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells
-
MC-CPA gene expression is about 2fold upregulated by bacterial lipopolysaccharide
-
TH2-high asthma cells are characterized by expression of CPA3
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y248A
-
the ratio of turnover number to Km-value with hippuryl-L-Phe as substrate is 113fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with N-[3-(2-furyl)acryloyl]-Phe-Phe as substrate is 262fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate as substrate is 85fold lower than that of the wild-type enzyme. The Ki-value for (2R,3S)-2-benzyl-3,4-epoxybutanoic acid is 3.1fold higher than the wild-type value
Y248F
-
the ratio of turnover number to Km-value with hippuryl-L-Phe as substrate is 49fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with N-[3-(2-furyl)acryloyl]-Phe-Phe as substrate is 49fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with O-(trans-p-chlorocinnamoyl)-L-beta-phenyllactate as substrate is 52.4fold lower than that of the wild-type enzyme, the ratio of turnover number to Km-value with hippuryl-DL-beta-phenyllactate as substrate is 6.5fold lower than that of the wild-type enzyme.The Ki-value for (2R,3S)-2-benzyl-3,4-epoxybutanoic acid is 86% of the wild-type value
A305E
-
tested Canavan Disease mutation, results in undetectable enzyme activity
A57T
-
untested Canavan Disease mutation, results in undetectable enzyme activity
C124A
-
alanine substitution of Cys124, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding
C152A
-
alanine substitution of Cys152, residue indicates by homology modelling to be in close proximity and in the proper orientation for disufide bonding
C152W
-
tested Canavan Disease mutation, results in undetectable enzyme activity
C61A
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
C61S
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
C61W
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
D204H
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
D249V
-
tested Canavan Disease mutation, results in undetectable enzyme activity
D68A
-
tested Canavan Disease mutation, results in undetectable enzyme activity
E178A
-
mutation of the general proton donor
E214X
-
tested Canavan Disease mutation, results in undetectable enzyme activity
E24D
-
mutation of a putative zinc-binding residue
E24G
-
mutation of a putative zinc-binding residue, tested Canavan Disease mutation, results in undetectable enzyme activity
E24H
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
E24H/H116E
-
mutant designed to switch the order of the zinc-binding residues
E285A
-
tested Canavan Disease mutation
F295S
-
untested Canavan Disease mutation, results in undetectable enzyme activity
G274R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
H116E
-
mutant for analyzing the biochemical basis for undetectable ASPA activity, and for testing of the hypothesis, that ASPA is a zinc-dependent metalloenzyme
H116G
-
mutation of a putative zinc-binding residue
H21E/E24H
-
mutant designed to switch the order of the zinc-binding residues
H21G
-
mutation of a putative zinc-binding residue
H21P
-
untested Canavan Disease mutation, results in undetectable enzyme activity
I143T
-
untested Canavan Disease mutation, results in undetectable enzyme activity
K213E/G274R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
M195R
-
untested Canavan Disease mutation, results in undetectable enzyme activity
P183H
-
untested Canavan Disease mutation
R127A
-
the mutation causes kcat to decrease from 12 to 0.012 which corresponds to a 6 kcal/mol decrease in the stabilization of transition state in the rate determining step
R63N
-
mutation that affects transition state stabilization
R71N
-
mutation that affects substrate carboxyl binding
Y356L
-
Tyr356 is crucial for ligand binding and hydrolysis of substrate peptide bond
E378A
-
Glu378 is crucial for ligand binding and hydrolysis of substrate peptide bond
additional information
-
mice lacking Nna1/CCP1 show absence of the detyrosinylated form of alpha-tubulin in mitral cells
additional information
-
in agiotensin-converting enzyme -/- mice the addition of the carboxypeptidase A inhibitor benzylsuccinate essentially abolishs the formation of Ang(1-9) and increases the levels of angiotensin I in cardiac membranes
Y356L/E378A
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mutant expresses about 80% of the amount of Mc-cpa compared to the wild type enzyme, the mutant enzyme lacks activity
additional information
Mus musculus C57B6
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mice lacking Nna1/CCP1 show absence of the detyrosinylated form of alpha-tubulin in mitral cells
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reversible denaturation: up to at least 7 M urea, irreversible: 33% ethanol-water mixture
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the purified protein is refolded in the deionized water for 16 h at 4C
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
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the application of the novel ochratoxin A hydrolytic enzyme to reduce the ochratoxin A contents on some food or feed products is under evaluation
analysis
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the enzyme serves as model enzyme for design of specific inhibiors for zinc proteases
biotechnology
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multi-block, surfactant copolymers are suitable for applications in which refolding of denaturated or misfolded proteins and suppression of aggregation are important objects
drug development
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the enzyme is a target for drug development for biotechnological and biomedical applications
drug development
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the enzyme serves as model enzyme for design of specific inhibiors for zinc proteases
food industry
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Brassica carinata protein hydrolysates could be used for developing functional foods for the treatment of heart and related diseases
food industry
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hydrolyzates could be used for preparing special diets when there is a need to increase the supply of branched amino acids and/or reduce the intake of aromatic amino acids
medicine
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design of mechanism-based, specific inhibitors to cure disease caused by enzyme overfunction
medicine
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increased activity of carboxypeptidase A has been demonstrated in plasma samples from patients with pancreatitis
medicine
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the avidin-biotin-PEGylated-carboxypeptidase complex has a great potential as a therapeutic protein delivery system for solid tumor prodrug targeting
pharmacology
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construction of synthetic artificial protease with substrate selectivity for CPA as a substrate, designing of the catalyst by use of specific CPA inhibitors, the artificial catalyst can be used as drug with the target being a protein or peptide related to a disease, overview
synthesis
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enzymatic modification of human haemoglobin, useful for functional studies
synthesis
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immobilization for synthetic use, useful tools for peptide biosynthesis in non-conventional media, considered
analysis
P15088
the enzyme can serve as specific molecular maker for mast cells amongst normal hematopoietic cell populations
medicine
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evaluation of an antibody-directed enzyme-prodrug therapy for anticancer treatment using the A33 antigen, the enzyme, and methotrexate-phenylalanine as prodrug, overview
medicine
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assay of total-carboxypeptidase A, the active form of CPA and pro CPA, in serum might be useful for the surveillance of early-stage pancreatic carcinoma
medicine
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carboxypeptidase A is an interesting biomedical target enzyme as it is involved in prostate cancer
medicine
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fusion protein design is successful in providing targeted inhibition of tumor growth in prostate cancer, the design can be used to construct other fusion genes
medicine
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mast cell-proteases are considered as promising drug targets
medicine
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mutations that results in near undetectable activity of aspartocyclase correlate with Canavan Disease, a neurodegenerative disorder usually fatal during childhood
medicine
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mc-CPA is an essential effector molecule providing a very rapid and life-saving response of toxin neutralization in vivo
medicine
P00731
results offer new opportunities for intervention and therapy of initiation and progression of autoimmune diseases
drug development
Q6ZXB9
potential target for drug development
medicine
Q9UI42
engaged in prostate cancer
additional information
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PTD012 might not belong to the carboxypeptidase family of enzymes, might belong to the superfamily of metallo-beta-lactamase fold proteins