2.6.1.96: 4-aminobutyrate-pyruvate transaminase
This is an abbreviated version!
For detailed information about 4-aminobutyrate-pyruvate transaminase, go to the full flat file.
Word Map on EC 2.6.1.96
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2.6.1.96
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gamma-aminobutyric
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2.6.1.19
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putrescine
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transaminases
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2-oxoglutarate
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taurine
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pyridoxal
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2-aminoethylphosphonic
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epilepsy
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semialdehyde
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ethanolamine-o-sulphate
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myelin
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polyamine
- 2.6.1.96
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gamma-aminobutyric
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2.6.1.19
- putrescine
- transaminases
- 2-oxoglutarate
- taurine
- pyridoxal
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2-aminoethylphosphonic
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epilepsy
- semialdehyde
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ethanolamine-o-sulphate
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myelin
- polyamine
Reaction
Synonyms
4-aminobutyrate transaminase, BnaA.GABA-T.a, BnaA.GABA-T.b, BnaA01g24820D, BnaA05g17430D, BnaC.GABA-T.a, BnaC.GABA-T.b, BnaC05g30410D, GABA transaminase, GABA-T, GABA-T2, GABA-T3, gaba:pyruvate transaminase, GABA:pyruvate-T, gamma-aminobutyrate transaminase, gamma-aminobutyrate transaminase 1, mitochondrial, gamma-aminobutyric acid pyruvate transaminase, gamma-aminobutyric acid transaminase, gammaaAminobutyric acid transaminase, Os04g0614500, Osl2, Pop2, pyruvate-specific mitochondrial GABA-T
ECTree
2.6.1.96 4-aminobutyrate-pyruvate transaminaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.6.1.96 - 4-aminobutyrate-pyruvate transaminase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-aminobutanoate + glyoxylate
succinate semialdehyde + glycine
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-
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ir
4-aminobutanoate + glyoxylate
succinate semialdehyde + glycine
the glyoxylate-dependent reaction is not reversible, although glyoxylate can also be used in conjunction with alanine as a substrate in the reverse reaction
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ir
4-aminobutanoate + glyoxylate
succinate semialdehyde + glycine
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-
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ir
4-aminobutanoate + glyoxylate
succinate semialdehyde + glycine
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-
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ir
4-aminobutanoate + glyoxylate
succinate semialdehyde + glycine
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-
-
?
4-aminobutanoate + glyoxylate
succinate semialdehyde + glycine
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-
-
?
4-aminobutanoate + glyoxylate
succinate semialdehyde + glycine
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-
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?
4-aminobutanoate + glyoxylate
succinate semialdehyde + glycine
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-
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?
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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-
-
-
?
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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-
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?
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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-
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r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
the pyruvate-dependent GABA-T reaction is reversible
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r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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-
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?
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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pyruvate-specific mitochondrial GABA-T
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r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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-
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r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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pyruvate-specific mitochondrial GABA-T
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r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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-
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?
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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-
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?
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
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-
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?
additional information
?
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GABA-T catalyses the breakdown of GABA to succinic semialdehyde. The enzyme shows both pyruvate- and glyoxylate-dependent activities, but no activity with 2-oxoglutarate. The substrate specificity at pH 9 reveals that the enzyme utilizes glyoxylate, as well as pyruvate, as amino acceptors in the forward reaction, and GABA, but not beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors
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-
?
additional information
?
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GABA-T catalyses the breakdown of GABA to succinic semialdehyde. The enzyme shows both pyruvate- and glyoxylate-dependent activities, but no activity with 2-oxoglutarate. The substrate specificity at pH 9 reveals that the enzyme utilizes glyoxylate, as well as pyruvate, as amino acceptors in the forward reaction, and GABA, but not beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors
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-
?
additional information
?
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GABA-T catalyses the breakdown of GABA to succinic semialdehyde. The enzyme shows both pyruvate- and glyoxylate-dependent activities, but no activity with 2-oxoglutarate. The substrate specificity at pH 9 reveals that the enzyme utilizes glyoxylate, as well as pyruvate, as amino acceptors in the forward reaction, and GABA, but not beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors
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?
additional information
?
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enzyme utilizes pyruvate and glyoxylate, but not 2-oxoglutarate
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?
additional information
?
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GABA-T isozymes catalyse the breakdown of GABA to succinic semialdehyde. The isozymes all have both pyruvate- and glyoxylate-dependent activities, and utilize GABA and Ala but not beta-Ala, Orn, acetylornithine, Ser, Gly, Asn, Gln, Glu, Val, Leu, Ile, Met, Phe, His, Lys, Arg, Asp, Thr, Tyr, Trp, Pro, or Cys as amino donors
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-
?
additional information
?
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GABA-T isozymes catalyse the breakdown of GABA to succinic semialdehyde. The isozymes all have both pyruvate- and glyoxylate-dependent activities, and utilize GABA and Ala but not beta-Ala, Orn, acetylornithine, Ser, Gly, Asn, Gln, Glu, Val, Leu, Ile, Met, Phe, His, Lys, Arg, Asp, Thr, Tyr, Trp, Pro, or Cys as amino donors
-
-
?
additional information
?
-
GABA-T isozymes catalyse the breakdown of GABA to succinic semialdehyde. The isozymes all have both pyruvate- and glyoxylate-dependent activities, and utilize GABA and Ala but not beta-Ala, Orn, acetylornithine, Ser, Gly, Asn, Gln, Glu, Val, Leu, Ile, Met, Phe, His, Lys, Arg, Asp, Thr, Tyr, Trp, Pro, or Cys as amino donors
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?
