Information on EC 1.14.11.17 - taurine dioxygenase

New: Word Map on EC 1.14.11.17
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

SplaateEC_Number,Commentary
EC NUMBER
COMMENTARY
1.14.11.17
-
SplaateRecommended_Name,GO_Number
RECOMMENDED NAME
GeneOntology No.
taurine dioxygenase
-
SplaateReaction,Reaction_id,Commentary,IF(Commentary != '',Organism,'') ,IF(Commentary != '',Literature,'')
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
-
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
mechanism
-
taurine + 2-oxoglutarate + O2 = sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
the TauD mechanism begins with the bidentate coordination of 2-oxoglutarate to Fe(II) displacing two water ligands. Taurine then binds to the active site resulting in the displacement of the apical H2O and formation of a 5-coordinate Fe(II) center. O2 binds to the open coordination site on Fe(II), yielding an Fe(III)-superoxo species. Subsequent oxidative decarboxylation of 2-oxoglutarate leads to formation of a Fe(IV)=O intermediate that triggers hydroxylation of the C1 carbon of taurine via hydrogen atom abstraction and radical rebound chemistry The hydroxylated taurine spontaneously decomposes to sulfite and aminoacetaldehyde
-
SplaateReaction_Type,Organism,Commentary,Literature
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
decarboxylation
-
-
dioxygenation
-
-
hydroxylation
-
the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
hydroxylation
-
catalyzes the hydroxylation of taurine to generate sulfite and aminoacetaldehyde in the presence of O2, alpha-ketoglutarate, and Fe(II)
hydroxylation
-
-
hydroxylation
-
-
hydroxylation
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
-
the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, alpha-ketoglutarate
SplaatePathway,BRENDA_Link,KEGG_Link,MetaCyc_Link,Source_Database
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
taurine degradation IV
-
-
taurine degradation
-
-
Taurine and hypotaurine metabolism
-
-
Sulfur metabolism
-
-
SplaateSystematic_Name,Commentary_IUBMB
SYSTEMATIC NAME
IUBMB Comments
taurine, 2-oxoglutarate:O2 oxidoreductase (sulfite-forming)
Requires FeII. The enzyme from Escherichia coli also acts on pentanesulfonate, 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2-yl)ethanesulfonate, but at lower rates.
SplaateSynonyms,Organism,Commentary,Literature
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-aminoethanesulfonate dioxygenase
-
-
-
-
2-aminoethanesulfonic acid/alpha-ketoglutarate dioxygenase
-
-
alpha-ketoglutarate-dependent dioxygenase
-
-
alpha-ketoglutarate-dependent dioxygenase
Pseudomonas putida S-313
-
-
-
alpha-ketoglutarate-dependent taurine dioxygenase
-
-
-
-
AtsK
Pseudomonas putida S-313
-
-
-
Fe(II)/2-oxoglutarate-dependent taurine dioxygenase
-
-
Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenase
-
-
Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenase
-
oxygenative alkylsulfatase
-
-
oxygenative alkylsulfatase
Pseudomonas putida S-313
-
-
-
SSI3
-
-
-
-
TauD
-
-
TauD
-
-
TauD-{FeNO}7
-
-
taurine (2-aminoethanesulfonate)/2-oxoglutarate dioxygenase
-
-
taurine alpha ketoglutarate dioxygenase
-
-
taurine alpha-ketoglutarate dioxygenase
-
-
taurine dioxygenase
-
-
taurine hydroxylase
-
-
taurine-alpha-ketoglutarate dioxygenase
-
taurine/2-oxoglutarate dioxygenase
-
-
taurine/alpha-ketoglutarate dioxygenase
-
-
taurine/alpha-ketoglutarate dioxygenase
-
-
taurine/alpha-ketoglutarate-dependent dioxygenase
-
-
taurine/alphaKG dioxygenase
-
-
taurine/alphaKGD
-
-
taurine: alpha-ketoglutarate dioxygenase
-
-
taurine:alpha-ketoglutarate dioxygenase
-
-
SplaateCAS_Registry_Number,Commentary
CAS REGISTRY NUMBER
COMMENTARY
197809-75-9
-
297319-14-3
-
325506-70-5
-
SplaateOrganism, Commentary,Literature, Sequence_Code,Sequence_db,Textmining
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain MC4100
-
-
Manually annotated by BRENDA team
strain S-313
-
-
Manually annotated by BRENDA team
Pseudomonas putida S-313
strain S-313
-
-
Manually annotated by BRENDA team
SplaateGeneral_Information, Organism, Commentary, Literature
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
cysteine metabolism
physiological function
-
nonheme iron enzyme, activation of C-H bonds
physiological function
-
important in antibiotic biosynthesis, oxygen sensing, DNA repair, biodegradation of anthropogenic compounds
additional information
-
development of a colorimetric assay method, based on the measurement of sulfite using Ellman's reagent, i.e. 2.5 mM 5,5'-dithiobis(2-nitrobenzoic acid), for determination of taurine in commercially available beverages and some biological samples, overview
additional information
-
metal-to-ligand charge-transfer transition involving the 2-oxoglutarate ligand with a six-coordinate metal center. Taurine does not coordinate the Fe(II) ion, but binds in its close vicinity, leading to loss of the coordinating water molecule. This change of the six-coordinate to five-coordinate Fe(II) center causes a small perturbation of the absorption spectrum
additional information
metal-to-ligand charge-transfer transition involving the 2-oxoglutarate ligand with a six-coordinate metal center. Taurine does not coordinate the Fe(II) ion, but binds in its close vicinity, leading to loss of the coordinating water molecule. This change of the six-coordinate to five-coordinate Fe(II) center causes a small perturbation of the absorption spectrum
additional information
-
structure-activity analysis, modeling and simulations, overview. Modeling of TauD-(Fe-NO) complex and spectral analysis
SplaateSubstrates,Products,id,Organism_Substrates,Commentary_Substrates, Literature_Substrates, Commentary_Products, Literature_Products,Reversibility
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-dioxo-2-isoindolineenthanesulfonic acid + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
show the reaction diagram
-
-
-
?
2-oxoglutarate + 2-methylaminoethane-1-sulfonic acid + O2
methylaminoacetaldehyde + succinate + sulfite + CO2
show the reaction diagram
-
assay at pH 6.2, 30C
-
?
butanesulfonic acid + 2-oxoglutarate + O2
sulfite + butanal + succinate + CO2
show the reaction diagram
-
-
-
?
hexanesulfonic acid + 2-oxoglutarate + O2
sulfite + hexanal + succinate + CO2
show the reaction diagram
-
-
-
?
hexyl sulfate + 2-oxoglutarate + O2
hexanal + sulfite + succinate + CO2
show the reaction diagram
Pseudomonas putida, Pseudomonas putida S-313
-
-
-
?
N-methyltaurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + methylaminoacetaldehyde
show the reaction diagram
-
-
-
?
O2 + 2-oxoglutarate + taurine
?
show the reaction diagram
-
assay at pH 6.2, 30C
-
-
?
pentanesulfonic acid + 2-oxoglutarate + O2
sulfite + pentanal + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
no substrates are methanesulfonic acid, ethanesulfonic acid, isethionic acid, 2-bromoethanesulfonic acid, L-cysteic acid, sulfosuccinate, 4-aminobenzenesulfonic acid, 2-(4-pyridyl)ethanesulfonic acid, N-phenyltaurine
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
enables the use of taurine as sulfur source
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
enables the use of taurine as sulfur source
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
enables the use of taurine as sulfur source
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
reaction mechanism via two accumulating, kinetically competent intermediates upon reaction of the TauD:Fe(II):RKG:taurine complex with O2
-
?
taurine + 2-oxoglutarate + O2
CO2 + succinate + sulfite + aminoacetaldehyde
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
succinate + CO2 + aminoethanol + sulfite
show the reaction diagram
-
-
-
?
taurine + alpha-ketoadipate + O2
sulfite + aminoacetaldehyde + pentan-1,5-dioic acid + CO2
show the reaction diagram
-
alpha-ketoadipate is less active than 2-oxoglutarate, no activity with pyruvate, alpha-ketobutyrate, alpha-ketovalerate, alpha-ketocaproate, alpha-ketoisovalerate and oxalacetat
-
?
MOPS + 2-oxoglutarate + O2
sulfite + ? + succinate + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
Pseudomonas putida, Pseudomonas putida S-313
-
the AtsK enzyme is not involved in the utilization of taurine as a sulfur source
-
-
-
SplaateNatural_Substrates,Natural_Products,id,Organism_Substrates,Commentary_Substrates,Literature_Substrates,Commentary_Products,Literature_Products,Reversibility
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
Q88RA3
-
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
P37610
enables the use of taurine as sulfur source
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
enables the use of taurine as sulfur source
-
?
taurine + 2-oxoglutarate + O2
sulfite + aminoacetaldehyde + succinate + CO2
show the reaction diagram
-
enables the use of taurine as sulfur source
-
?
SplaateCofactor,Organism,Commentary,Literature,Filename
SplaateMetals_Ions,Organism,Commentary, Literature
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cr2+
-
Cr(II) replaces Fe2+ and binds stoichiometrically with 2-oxoglutarate to the Fe(II)/2-oxoglutarate binding site of the protein, with additional Cr(II) used to generate a chromophore attributed to a Cr(III)-semiquinone in a small percentage of the sample. Formation of the semiquinone requires the dihydroxyphenylalanine quinone form of Y73, generated by intracellular self-hydroxylation
Fe
-
the enzyme contains a central iron atom that is held in position by interactions with the side chains of two histidine and an aspartic acid residue
Fe
-
catalyzes the hydroxylation of taurine to generate sulfite and aminoacetaldehyde in the presence of O2, alpha-ketoglutarate, and Fe(II)
Fe2+
-
maximal activation between 0.005 and 0.150 mM
Fe2+
-
required, essential cofactor
Fe2+
-
required, bound in an open metal coordination site
Fe2+
-
required, forms iron-oxygen complex during the course of reaction
Fe2+
-
required for activity, highest activity in the presence of 0.1 mM
Fe2+
-
binding structure and role in the kinetic mechanism, overview
Fe2+
-
dependent on, mononuclear non-heme iron center, binding structure and kinetics, spectral analysis, overview
Fe2+
dependent on, mononuclear non-heme iron center, binding structure and kinetics, spectral analysis, overview
Fe2+
-
dependent on, non-heme mononuclear Fe(II) center
Fe3+
-
formation of Fe3+-oxyl species as intermediates
Iron
-
ferrous active site, analysis by circular dichroism and magnetic circular dichroism. The excited-state splittings and energies of the two transitions of TauD/FeII are consistent with a distorted 6C resting ferrous site. One of the six ligands is weakly coordinated, and 2-oxoglutarate is bound in a bidentate fashion
Iron
-
upon binding Fe(II), anaerobic samples of wild-type TauD and the three active variants generate a weak green chromophore resembling a catecholate-FeI(III)species. The quione oxidation state of dihydroxyphenylalanine reacts with Fe(II) to form this species
Iron
-
comparative quantum mechanics/molecular mechanics and density functional theory calculations on the oxo-iron species. Protonation of the histidine ligands of iron is essential to reproduce the correct electronic representations of the enzyme. Enzyme is very efficient in reacting with substrates via low reaction barriers
additional information
-
Mg2+, Ca2+, Mn2+ or Ni2+ can not replace iron
additional information
-
Ni2+, Co2+, Mn2+, Cu2+, Zn2+, Mg2+, and Ca2+ have no stimulatory effect
SplaateInhibitors, Organism, Commentary, Literature,Filename
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
-
inhibits activity by 80-95% at 0.01-0.05 mM
Co2+
-
IC50: 0.0019 mM, in the presence of Fe2+; IC50: 0.041 mM
Cu2+
-
inhibits activity by 80-95% at 0.01-0.05 mM
EDTA
-
complete inactivation
EDTA
-
0.1 mM EDTA abolishes activity completely
N-oxalylglycine
-
-
Ni2+
-
IC50: 0.00071 mM, in the presence of Fe2+; IC50: 0.032 mM
nonyl sulfate
-
inhibits at concentrations between 1 and 10 mM
SDS
-
inhibits at concentrations between 1 and 10 mM
Zn2+
-
inhibits activity by 80-95% at 0.01-0.05 mM
additional information
-
no reduction in enzyme activity is observed for sulfate concentrations up to 10 mM
-
SplaateActivating_Compound, Organism, Commentary, Literature,Filename
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
required for activity
ascorbate
-
50% increase in activity at 0.2-0.8 mM
ascorbate
-
3fold increase of activity at 0.2 mM
SplaateKM_Value,KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.485
1,3-dioxo-2-isoindolineenthanesulfonic acid
-
-
-
0.009
2-oxoglutarate
-
wild type enzyme, in the presence of taurine
0.011
2-oxoglutarate
-
-
0.012
2-oxoglutarate
-
mutant enzyme Y73I, in the presence of taurine
0.015
2-oxoglutarate
-
mutant enzyme Y73I, without taurine
0.02
2-oxoglutarate
-
wild type enzyme, without taurine
0.032
2-oxoglutarate
-
wild-type, 30C
0.048
2-oxoglutarate
-
mutant enzyme W98I, in the presence of taurine
0.055
2-oxoglutarate
-
mutant H255E, 30C
0.059
2-oxoglutarate
-
mutant H255Q, 30C
0.081
2-oxoglutarate
-
mutant D101E, 30C
1.49
butanesulfonic acid
-
-
1.51
hexanesulfonic acid
-
-
0.0051
N-methyltaurine
-
deuterated substrate
0.048
N-methyltaurine
-
commercially available substrate
0.054
N-methyltaurine
-
-
0.0056
O2
-
deuterated substrate 2-methyltaurine
0.041
O2
-
commercially available substrate 2-methyltaurine; substrate taurine
0.046
O2
-
substrate 2-methyltaurine
0.59
pentanesulfonic acid
-
-
0.019
taurine
-
mutant H255E, 30C; wild-type, 30C
0.0194
taurine
-
-
0.021
taurine
-
mutant H255Q, 30C
0.052
taurine
-
wild type enzyme
0.055
taurine
-
-
0.061
taurine
-
mutant D101E, 30C
0.145
MOPS
-
-
additional information
additional information
-
kinetic mechanism, overview
-
SplaateTurnover_Number, Turnover_Number_Maximum, Substrate,Organism,Commentary, Literature, Filename
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
2-oxoglutarate
Escherichia coli
-
wild type enzyme, without taurine
0.12
2-oxoglutarate
Escherichia coli
-
mutant enzyme Y73I, without taurine
0.14
2-oxoglutarate
Escherichia coli
-
mutant enzyme W98I, in the presence of taurine
1
2-oxoglutarate
Escherichia coli
-
mutant enzyme Y73I, in the presence of taurine
0.74
taurine
Escherichia coli
-
mutant D101E, 30C
1.1
taurine
Escherichia coli
-
mutant H255E, 30C
2.7
taurine
Escherichia coli
-
mutant H255Q, 30C
3
taurine
Escherichia coli
-
wild type enzyme
3.3
taurine
Escherichia coli
-
wild-type, 30C
3
2-oxoglutarate
Escherichia coli
-
wild type enzyme, in the presence of taurine
additional information
additional information
Pseudomonas putida
Q88RA3
real-time NMR spectra to follow enzymatic turnover
-
SplaateKCat_KM_Value,KCat_KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000001
O2
Escherichia coli
-
substrate 2-methyltaurine
9
0.000000011
O2
Escherichia coli
-
deuterated substrate 2-methyltaurine
9
0.000000012
O2
Escherichia coli
-
commercially available substrate 2-methyltaurine; sustrate taurine
9
1.01
O2
Bacteria
-
-
9
0.000000025
taurine
Escherichia coli
-
-
595
SplaateKI_Value,KI_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.29
N-oxalylglycine
-
-
SplaateIC50_Value,IC50_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0019
Co2+
Escherichia coli
-
IC50: 0.0019 mM, in the presence of Fe2+
0.041
Co2+
Escherichia coli
-
IC50: 0.041 mM
0.00071
Ni2+
Escherichia coli
-
IC50: 0.00071 mM, in the presence of Fe2+
0.032
Ni2+
Escherichia coli
-
IC50: 0.032 mM
SplaateSpecific_Activity, Specific_Activity_Maximum, Organism ,Commentary, Literature
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.012
-
strain MC4100 grown in sulfate-free minimal medium containing 0.25 mM taurine as sulfur source
1.64
-
purified enzyme
3.56
-
purified enzyme, pH and temperature not specified in the publication
8.11
purified enzyme, pH and temperature not specified in the publication
SplaatepH_Optimum, pH_Optimum_Maximum, Organism, Commentary, Literature
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
-
assay at
6.2
-
assay at
7
-
in Tris-acetate buffer
7
-
assay at
SplaatepH_Range,pH_Range_Maximum, Organism,Commentary, Literature
SplaateTemperature_Optimum, Temperature_Optimum_Maximum, Organism, Commentary, Literature
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
SplaateTemperature_Range, Temperature_Range_Maximum, Organism, Commentary, Literature
SplaatepI_Value,pI_Value_Maximum, Organism,Commentary, Literature
SplaateSource_Tissue, Organism, Commentary, Literature, Textmining
SplaateLocalization, Organism, Commentary, id_go, Literature, Textmining
SplaatePDB,PDB,PDB,Organism,Uniprot_ID
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium avium (strain 104)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Pseudomonas putida (strain KT2440)
Pseudomonas putida (strain KT2440)
Pseudomonas putida (strain KT2440)
SplaateMolecular_Weight, Molecular_Weight_Maximum, Organism, Commentary, Literature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
-
-
673443
32410
-
calculation from gene sequence
285263
37400
-
estimated by SDS-PAGE
285263
81000
-
gel filtration on Superose 6 and Superose 12 HR
285263
110000
-
gel filtration
724974
112000
gel filtration
724974
120000
sedimentation velocity analytical ultracentrifugation
724974
121000
-
gel filtration
680611
127000
-
sedimentation velocity analytical ultracentrifugation
724974
SplaateSubunits, Organism, Commentary, Literature
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 37400, SDS-PAGE
dimer
-
crystal structure analysis
homotetramer
-
4 * 30250, gel filtration; 4 * 32000, SDS-PAGE
tetramer
-
4 * 32000, about, sequence calculation, TauDEc is a tetramer in solution and in the crystals, gel filtration and sedimentation velocity analytical ultracentrifugation
tetramer
4 * 31000, about, sequence calculation, TauDPp is a tetramer in solution and in the crystals
homotetramer
Pseudomonas putida S-313
-
4 * 30250, gel filtration; 4 * 32000, SDS-PAGE
-
additional information
-
Geometric Structure of TauD-{FeNO}7, overview
additional information
topology of an apo-TauDPp monomer,overview
SplaatePosttranslational_Modification, Organism, Commentary, Literature
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Trp128, Trp240, and Trp248 are hydroxylated upon exposure to oxygen
SplaateCommentary, Organism, Literature
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
comparative quantum mechanics/molecular mechanics and density functional theory calculations on the oxo-iron species. Protonation of the histidine ligands of iron is essential to reproduce the correct electronic representations of the enzyme. Enzyme is very efficient in reacting with substrates via low reaction barriers
-
density functional theory calculations based on a series of models for the key intermediate with the Fe(IV) ion coordinated by the expected two imidazoles from His99 and His255, two carboxylates, succinate and Asp101, and oxo ligands. Calculated parameters of distorted octahedral models for the intermediate, in which one of the carboxylates serves as a monodentate ligand and the other as a bidentate ligand, and a trigonal bipyramidal model, in which both carboxylates serve as monodentate ligands, agree well with the experimental parameters
-
electron spin echo-detected EPR spectrum ESE and deuterium electron spin echo envelope modulation spectrum ESEEM of the Fe(II)-NO form of the enzyme treated with 2-oxoglutarate and taurine
-
enzyme with bound substrate taurine, crystal structure analysis at 2.5 A resolution
-
hanging drop method, inclusion of taurine and 2-oxoglutarate is absolutely required for crystal formation
-
presence of taurine is required for crystal growth
-
three crystal structures of the apo form, vapor diffusion techniques, protein solution contains 1. 27-28 m/ml TauDPp in 25 mM Tris-HCl, pH 7.7, or 2. 21 mg/ml TauDPp in 25 mM Tris-HCl pH 7.7, containing 10 mM taurine, 0.1 M (NH4)2SO4 and 20% v?v glycerol, mixed with reservoir solution containing 1. 15% w?v PEG 1000, 40% v?v PEG 400, 0.15 M NaK phosphate, and 0.1 M imidazole chloride, pH 6.5, or 2. 20% w?v PEG 5000 monomethyl ether, 0.1 M Bis-Tris-HCl, pH 6.5, X-ray diffraction structure determination and analysis at 1.85-2.6 A resolution
SplaatepH_Stability,pH_Stability_Maximum, Organism, Commentary, Literature
SplaateTemperature_Stability,Temperature_Stability_Maximum, Organism, Commentary, Literature
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
incubation at 30C leads to rapid inactivation, effect is enhanced by ascorbate and not due to oxidation of the enzyme-bound ferrous iron
285263
SplaateGeneral_Stability, Organism, Literature
SplaateOrganic_Solvent, Organism, Commentary, Literature
SplaateOxidation_Stability,Organism,Literature
SplaateStorage_Stability, Organism, Literature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, phosphate buffer, 16% glycerol, 10 weeks, activity increases 4-fold
-
-20C, phosphate buffer, without glycerol, 3 weeks, more than 50% loss of activity
-
SplaateCommentary, Organism, Literature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography and HP phenyl-Sepharose column chromatography
-
dialysis against 25 mM Tris buffer at pH 8.0
-
recombinant His-tagged TauD from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant protein using His-tag
-
two-step purification from overexpressing Escherichia coli to apparent homogeneity
-
Resource-Q anion-exchange column chromatography and Superdex 200 gel filtration
-
SplaateCommentary, Organism, Literature
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as His-tag fusion protein
-
expression of His-tagged TauD in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
expression of TauD in Escherichia coli strains BL21(DE3) and Rosetta Blue(DE3)
SplaateCommentary, Organism, Literature
SplaateEngineering, Organism, Commentary, Literature
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D101A
-
no catalytic activity
D101C
-
no catalytic activity
D101E
-
about 3-fold increase in Km values
D101H
-
no catalytic activity
D101N
-
no catalytic activity
D101Q
-
no catalytic activity
F159A
-
decrease in coupling of oxygen activation to C-H cleavage
F159G
-
decrease in coupling of oxygen activation to C-H cleavage
F159L
-
decrease in coupling of oxygen activation to C-H cleavage
F159V
-
decrease in coupling of oxygen activation to C-H cleavage
H255A
-
no catalytic activity
H255C
-
no catalytic activity
H255D
-
no catalytic activity
H255E
-
about 2-fold increase in Km value of 2-oxoglutarate
H255N
-
no catalytic activity
H255Q
-
about 2-fold increase in Km value of 2-oxoglutarate
H99A
-
replacement of the residue that contributes the imidazole ligand cis to the oxo group. Density functional theory calculations show that the imidazole is replaced by a water ligand
H99A
-
no catalytic activity
H99C
-
no catalytic activity
H99D
-
no catalytic activity
H99E
-
no catalytic activity
H99N
-
no catalytic activity
H99Q
-
no catalytic activity
W98I
-
reduced activity compared to the wild type enzyme
Y73F
-
active, but mutant is incapable of formation of a Cr(III)-semiquinone chromophore
Y73I
-
reduced activity compared to the wild type enzyme
SplaateCommentary, Organism, Literature
SplaateApplication,Organism,Commentary,Literature
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
development of a colorimetric assay method for determination of taurine in commercially available beverages and some biological samples using the taurine dioxygenase. Taurine determination in food control, biological research, and diagnoses based on urinary taurine concentration
biotechnology
-
model system for non-heme iron oxygenases