2.6.1.55: taurine-2-oxoglutarate transaminase
This is an abbreviated version!
For detailed information about taurine-2-oxoglutarate transaminase, go to the full flat file.
Word Map on EC 2.6.1.55
-
2.6.1.55
-
transamination
-
sulfoacetaldehyde
-
hypotaurine
-
sulfonate
-
isethionate
-
pyridoxal
-
2-aminoethanesulfonate
- 2.6.1.55
-
transamination
- sulfoacetaldehyde
- hypotaurine
- sulfonate
- isethionate
- pyridoxal
-
2-aminoethanesulfonate
Reaction
Synonyms
aminotransferase, taurine, BkToa, taurine transaminase, taurine-alpha-ketoglutarate aminotransferase, taurine-glutamate transaminase, taurine:2-oxoglutarate aminotransferase, taurine:alpha-ketoglutarate aminotransferase
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Substrates Products
Substrates Products on EC 2.6.1.55 - taurine-2-oxoglutarate transaminase
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REACTION DIAGRAM
4-aminobutyrate + 2-oxoglutarate
L-glutamate + acetaldehyde + sulfite
Achromobacter superficialis
-
60% of the activity with taurine
-
-
?
2-oxopropanesulfonate + L-glutamate
Achromobacter polymorph
-
-
-
?
3-aminopropanesulfonate + 2-oxoglutarate
2-oxopropanesulfonate + L-glutamate
Achromobacter superficialis
-
-
-
?
3-aminopropanesulfonate + 2-oxoglutarate
2-oxopropanesulfonate + L-glutamate
Achromobacter superficialis
-
43% of the activity with taurine
-
?
3-aminopropanesulfonate + 2-oxoglutarate
2-oxopropanesulfonate + L-glutamate
Achromobacter superficialis
-
43% of the activity with taurine
-
?
3-oxopropanoate + L-glutamate
Achromobacter polymorph
-
-
-
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter polymorph KR B-88
-
-
-
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
-
-
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
-
-
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
184% of the activity with taurine
-
?
beta-alanine + 2-oxoglutarate
3-oxopropanoate + L-glutamate
Achromobacter superficialis ICR-B-89
-
184% of the activity with taurine
-
?
3-oxobutyrate + L-glutamate
Achromobacter superficialis
-
14% of the activity with taurine
-
?
DL-3-aminobutyrate + 2-oxoglutarate
3-oxobutyrate + L-glutamate
Achromobacter superficialis
-
14% of the activity with taurine
-
?
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter polymorph
-
-
-
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter polymorph KR B-88
-
-
-
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
-
-
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
-
-
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter superficialis
-
208% of the activity with taurine
-
?
DL-3-aminoisobutyrate + 2-oxoglutarate
2-methyl-3-oxopropanoate + L-glutamate
Achromobacter superficialis ICR-B-89
-
208% of the activity with taurine
-
?
2-oxoethanesulfinic acid + L-glutamate
Achromobacter polymorph
-
-
-
?
hypotaurine + 2-oxoglutarate
2-oxoethanesulfinic acid + L-glutamate
Achromobacter polymorph KR B-88
-
-
-
?
hypotaurine + 2-oxoglutarate
2-oxoethanesulfinic acid + L-glutamate
Achromobacter superficialis
-
601% of the activity with taurine
-
?
hypotaurine + 2-oxoglutarate
2-oxoethanesulfinic acid + L-glutamate
Achromobacter superficialis
-
601% of the activity with taurine
-
?
hypotaurine + 2-oxoglutarate
2-oxoethanesulfinic acid + L-glutamate
Achromobacter superficialis
-
6 times the rate of taurin transamination
-
?
2-sulfoacetaldehyde + L-glutamate
2-oxoglutarate is the physiological acceptor
-
-
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
the enzyme BkToa from Bifidobacterium kashiwanohense shows high specificity for 2-oxoglutarate as the amine acceptor, pyruvate does not function as acceptor
-
-
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
2-oxoglutarate is the physiological acceptor
-
-
?
taurine + 2-oxoglutarate
2-sulfoacetaldehyde + L-glutamate
the enzyme BkToa from Bifidobacterium kashiwanohense shows high specificity for 2-oxoglutarate as the amine acceptor, pyruvate does not function as acceptor
-
-
?
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph
-
-
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph
-
no activity with L- and D-amino acids
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph
-
no activity with pyruvate, phenylpyruvate, oxaloacetate
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph KR B-88
-
no activity with L- and D-amino acids
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph KR B-88
-
no activity with pyruvate, phenylpyruvate, oxaloacetate
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter polymorph KR B-88
-
-
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
-
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
no activity with aminomethanesulfonate, glycine, 5-aminopentanoate and amines
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
no activity with L- and D-amino acids
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
no activity with pyruvate, phenylpyruvate, oxaloacetate
-
?
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
no activity with pyruvate, phenylpyruvate, oxaloacetate
-
-
?
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis
-
no activity with pyruvate, phenylpyruvate, oxaloacetate
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis ICR-B-89
-
no activity with aminomethanesulfonate, glycine, 5-aminopentanoate and amines
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis ICR-B-89
-
no activity with L- and D-amino acids
-
r
taurine + 2-oxoglutarate
sulfoacetaldehyde + L-glutamate
Achromobacter superficialis ICR-B-89
-
no activity with pyruvate, phenylpyruvate, oxaloacetate
-
r
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-