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Information on EC 2.6.1.55 - taurine-2-oxoglutarate transaminase
for references in articles please use BRENDA:EC2.6.1.55
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EC Tree 2 Transferases
2.6 Transferring nitrogenous groups
2.6.1 Transaminases
2.6.1.55 taurine-2-oxoglutarate transaminase
IUBMB Comments
A pyridoxal-phosphate protein. Also acts on D,L-3-amino-isobutanoate, β-alanine and 3-aminopropanesulfonate. Involved in the microbial utilization of β-alanine.
The expected taxonomic range for this enzyme is: Bifidobacterium catenulatum subsp. kashiwanohense
- 2.6.1.55
-
transamination
- sulfoacetaldehyde
- hypotaurine
- sulfonate
- isethionate
- pyridoxal
-
2-aminoethanesulfonate
showSynonyms
bktoa, taurine transaminase, taurine:2-oxoglutarate aminotransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminotransferase, taurine
-
-
-
-
BkToa
taurine transaminase
-
-
-
-
taurine-alpha-ketoglutarate aminotransferase
-
-
-
-
taurine-glutamate transaminase
-
-
-
-
taurine:2-oxoglutarate aminotransferase
taurine:alpha-ketoglutarate aminotransferase
-
-
-
-
taurine:2-oxoglutarate aminotransferase
-
taurine:2-oxoglutarate aminotransferase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
taurine + 2-oxoglutarate = 2-sulfoacetaldehyde + L-glutamate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
taurine degradation III
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SYSTEMATIC NAME
IUBMB Comments
taurine:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein. Also acts on D,L-3-amino-isobutanoate, beta-alanine and 3-aminopropanesulfonate. Involved in the microbial utilization of beta-alanine.
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CAS REGISTRY NUMBER
COMMENTARY
9076-52-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-aminobutyrate + 2-oxoglutarate
L-glutamate + acetaldehyde + sulfite
Achromobacter superficialis
-
Substrates: 60% of the activity with taurine
Products: -
Products: -
?
DL-3-aminobutyrate + 2-oxoglutarate
3-oxobutyrate + L-glutamate
Achromobacter superficialis
-
Substrates: 14% of the activity with taurine
Products: -
Products: -
?
3-aminopropanesulfonate + 2-oxoglutarate
2-oxopropanesulfonate + L-glutamate
Achromobacter polymorph
-
Substrates: -
Products: -
Products: -
?
3-aminopropanesulfonate + 2-oxoglutarate
2-oxopropanesulfonate + L-glutamate
Achromobacter superficialis
-
Substrates: -
Products: -
Products: -
?
3-aminopropanesulfonate + 2-oxoglutarate
2-oxopropanesulfonate + L-glutamate
Achromobacter superficialis
-
Substrates: 43% of the activity with taurine
Products: -
Products: -
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter polymorph
-
Substrates: -
Products: -
Products: -
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter polymorph KR B-88
-
Substrates: -
Products: -
Products: -
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
Substrates: -
Products: -
Products: -
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
Substrates: 184% of the activity with taurine
Products: -
Products: -
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter superficialis ICR-B-89
-
Substrates: 184% of the activity with taurine
Products: -
Products: -
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter polymorph
-
Substrates: -
Products: -
Products: -
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter polymorph KR B-88
-
Substrates: -
Products: -
Products: -
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
Substrates: -
Products: -
Products: -
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
Substrates: 208% of the activity with taurine
Products: -
Products: -
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter superficialis ICR-B-89
-
Substrates: 208% of the activity with taurine
Products: -
Products: -
?
hypotaurine + 2-oxoglutarate
2-oxoethanesulfinic acid + L-glutamate
Achromobacter polymorph
-
Substrates: -
Products: -
Products: -
?
hypotaurine + 2-oxoglutarate
2-oxoethanesulfinic acid + L-glutamate
Achromobacter polymorph KR B-88
-
Substrates: -
Products: -
Products: -
?
hypotaurine + 2-oxoglutarate
2-oxoethanesulfinic acid + L-glutamate
Achromobacter superficialis
-
Substrates: 601% of the activity with taurine
Products: -
Products: -
?
hypotaurine + 2-oxoglutarate
2-oxoethanesulfinic acid + L-glutamate
Achromobacter superficialis
-
Substrates: 6 times the rate of taurin transamination
Products: -
Products: -
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
Substrates: 2-oxoglutarate is the physiological acceptor
Products: -
Products: -
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
Substrates: the enzyme BkToa from Bifidobacterium kashiwanohense shows high specificity for 2-oxoglutarate as the amine acceptor, pyruvate does not function as acceptor
Products: -
Products: -
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
Substrates: 2-oxoglutarate is the physiological acceptor
Products: -
Products: -
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
Substrates: the enzyme BkToa from Bifidobacterium kashiwanohense shows high specificity for 2-oxoglutarate as the amine acceptor, pyruvate does not function as acceptor
Products: -
Products: -
?
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph
-
Substrates: -
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph
-
Substrates: no activity with L- and D-amino acids
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph
-
Substrates: no activity with pyruvate, phenylpyruvate, oxaloacetate
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph KR B-88
-
Substrates: no activity with L- and D-amino acids
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph KR B-88
-
Substrates: no activity with pyruvate, phenylpyruvate, oxaloacetate
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph KR B-88
-
Substrates: -
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
Substrates: -
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
Substrates: no activity with aminomethanesulfonate, glycine, 5-aminopentanoate and amines
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
Substrates: no activity with L- and D-amino acids
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
Substrates: no activity with pyruvate, phenylpyruvate, oxaloacetate
Products: -
Products: -
?
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
Substrates: no activity with pyruvate, phenylpyruvate, oxaloacetate
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
Substrates: no activity with pyruvate, phenylpyruvate, oxaloacetate
Products: -
Products: -
?
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis ICR-B-89
-
Substrates: no activity with aminomethanesulfonate, glycine, 5-aminopentanoate and amines
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis ICR-B-89
-
Substrates: no activity with L- and D-amino acids
Products: -
Products: -
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis ICR-B-89
-
Substrates: no activity with pyruvate, phenylpyruvate, oxaloacetate
Products: -
Products: -
r
additional information
?
-
Substrates: in the enzyme complex crystal structure, two glutamate molecules are bound in sites near the predicted active site and they may occupy a path for substrate entry and product release
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the enzyme complex crystal structure, two glutamate molecules are bound in sites near the predicted active site and they may occupy a path for substrate entry and product release
Products: -
Products: -
?
additional information
?
-
Substrates: in the enzyme complex crystal structure, two glutamate molecules are bound in sites near the predicted active site and they may occupy a path for substrate entry and product release
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
Substrates: 2-oxoglutarate is the physiological acceptor
Products: -
Products: -
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
Substrates: 2-oxoglutarate is the physiological acceptor
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
Achromobacter superficialis
-
4 mol of pyridoxal phosphate per mol of enzyme
pyridoxal 5'-phosphate
Achromobacter superficialis
-
enzyme inactivated by treatment with ammonium sulfate is activated by incubation with pyridoxal 5'-phosphate at 45-60°C for about 10 min
pyridoxal 5'-phosphate
each monomer of the homodimeric enzyme exhibits a typical type I PLP-enzyme fold and conserved PLP-coordinating residues interacting with the pyridoxal 5'-phosphate (PLP) molecule, binding structure in the active site, modelling, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Methyl-2-benzothiazolone hydrazone hydrochloride
Achromobacter superficialis
-
weak inhibition
taurine-PLP aldimine
induced fit docking modelling. Lys279, a key residue in the pocket, is the receptor box center
additional information
Achromobacter superficialis
-
not inhibited by p-chloromercuribenzoate, monoiodoacetic acid, D-penicillamine, L-penicillamine and EDTA
-
additional information
Achromobacter superficialis
-
not inhibited by p-chloromercuribenzoate, monoiodoacetic acid, D-penicillamine, L-penicillamine and EDTA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
2-oxoglutarate
pH 7.2, 37°C, recombinant enzyme
11
2-oxoglutarate
Achromobacter superficialis
-
pH 8.0, 37°C, cosubstrate DL-3-aminoisobutyrate
1.1
taurine
pH 7.2, 37°C, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.7
2-oxoglutarate
pH 7.2, 37°C, recombinant enzyme
3.7
taurine
pH 7.2, 37°C, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.06
2-oxoglutarate
pH 7.2, 37°C, recombinant enzyme
3.36
taurine
pH 7.2, 37°C, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
coupled assay with glutamate dehydrogenase/alanine dehydrogenase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Achromobacter superficialis
isolated from human infant feces
UniProt
brenda
isolated from human infant feces
UniProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
sequence comparisons and phylogenetic analysis of taurine:oxoglutarate aminotransferases and taurine:pyruvate aminotransferases, overview
evolution
-
sequence comparisons and phylogenetic analysis of taurine:oxoglutarate aminotransferases and taurine:pyruvate aminotransferases, overview
-
metabolism
BkToa is part of a gene cluster putatively involved in taurine nitrogen assimilation. In this pathway, isothionate is formed by a sulfoacetaldehyde reductase TauF, a member of the metal-dependent alcohol dehydrogenase family
metabolism
-
BkToa is part of a gene cluster putatively involved in taurine nitrogen assimilation. In this pathway, isothionate is formed by a sulfoacetaldehyde reductase TauF, a member of the metal-dependent alcohol dehydrogenase family
-
physiological function
taurine is thought to serve as a source of carbon, nitrogen and sulfur for certain gut bacteria, particularly for strict anaerobes residing in the nutrient-poor environment of the distal gut. Taurine aminotransferases catalyze the first step in taurine catabolism in many taurine-degrading bacteria and play an important role in bacterial taurine metabolism in the mammalian gut
physiological function
-
taurine is thought to serve as a source of carbon, nitrogen and sulfur for certain gut bacteria, particularly for strict anaerobes residing in the nutrient-poor environment of the distal gut. Taurine aminotransferases catalyze the first step in taurine catabolism in many taurine-degrading bacteria and play an important role in bacterial taurine metabolism in the mammalian gut
-
additional information
molecular docking reveals a role for active site residues Trp21 and Arg156, conserved in Toa enzymes, in interacting with the sulfonate group of taurine
additional information
-
molecular docking reveals a role for active site residues Trp21 and Arg156, conserved in Toa enzymes, in interacting with the sulfonate group of taurine
additional information
-
molecular docking reveals a role for active site residues Trp21 and Arg156, conserved in Toa enzymes, in interacting with the sulfonate group of taurine
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A0A7I435_9BIFI
447
0
49593
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
109700
recombinant enzyme, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
additional information
homodimer
2 * 49600, about, sequence calculation
homodimer
-
2 * 49600, about, sequence calculation
-
additional information
each monomer exhibits a typical type I PLP-enzyme fold and conserved PLP-coordinating residues interacting with the pyridoxal 5'-phosphate (PLP) molecule
additional information
-
each monomer exhibits a typical type I PLP-enzyme fold and conserved PLP-coordinating residues interacting with the pyridoxal 5'-phosphate (PLP) molecule
additional information
-
each monomer exhibits a typical type I PLP-enzyme fold and conserved PLP-coordinating residues interacting with the pyridoxal 5'-phosphate (PLP) molecule
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with pyridoxal 5'-phosphate and glutamate, hanging-drop vapor diffusion method, mixing of 15 mg/ml protein solution with reservoir solution containing 0.1 M MES, pH 5.0, 0.2 M ammonium chloride, 20% w/v PEG 6000, 0.5 mM PLP, and 100 mM glutamate, X-ray diffraction structure determination and analysis at 2.7 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
treatment with ammonium sulfate during purification leads to a significant loss of activity
Achromobacter superficialis
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose, Sephadex G-150, hydroxylapatite, ammonium sulfate, Sephadex g-150, crystalization
Achromobacter superficialis
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the tag is cleaved off by TEV protease, followed by another step of nickel affinity chromatography, dialysis, and anion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AH68_00255, sequence comparisons and phylogenetic analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Toyama, S.; Misono, H.; Soda, K.
Crystalline taurine: alpha-ketoglutarate aminotransferase from Achromobacter superficialis
Biochem. Biophys. Res. Commun.
46
1374-1379
1972
Achromobacter superficialis
brenda
Yonaha, K.; Toyama, S.; Soda, K.
Taurine-glutamate transaminase
Methods Enzymol.
113
102-108
1985
Achromobacter superficialis, Achromobacter polymorph, Achromobacter superficialis ICR-B-89, Achromobacter polymorph KR B-88
brenda
Toyama, S.; Misono, H.; Soda, K.
Properties of taurine: alpha-ketoglutarate aminotransferase of Achromobacter superficialis. Inactivation and reactivation of enzyme
Biochim. Biophys. Acta
523
75-81
1978
Achromobacter superficialis
brenda
Toyama, S.; Soda, K.
Occurrence of taurine: alpha-ketoglutarate aminotransferase in bacterial extracts
J. Bacteriol.
109
533-538
1972
Achromobacter superficialis, Achromobacter polymorph, Achromobacter polymorph KR B-88
brenda
Tanaka, H.; Toyama, S.; Tsukahara, H.; Soda, K.
Transamination of hypotaurine by taurine:alpha-ketoglutarate aminotransferase
FEBS Lett.
45
111-113
1974
Achromobacter superficialis
brenda
Li, M.; Wei, Y.; Yin, J.; Lin, L.; Zhou, Y.; Hua, G.; Cao, P.; Ang, E.L.; Zhao, H.; Yuchi, Z.; Zhang, Y.
Biochemical and structural investigation of taurine 2-oxoglutarate aminotransferase from Bifidobacterium kashiwanohense
Biochem. J.
476
1605-1619
2019
Bifidobacterium catenulatum subsp. kashiwanohense (A0A0A7I435), Bifidobacterium catenulatum subsp. kashiwanohense, Bifidobacterium catenulatum subsp. kashiwanohense PV20-2 (A0A0A7I435)
brenda
EXTERNAL LINKS (specific for EC-Number 2.6.1.55)
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