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(1R,4S)-4-amino-2-cyclopentene-1-carboxylic acid + 2-oxoglutarate
? + L-glutamate
-
analogue of 4-aminobutanoate, vigabatrin
-
-
?
(4R)-4-amino-1-cyclopentene-1-carboxylic acid + 2-oxoglutarate
4-oxo-1-cyclopentene1-carboxylic acid + L-glutamate
-
analogue of 4-aminobutanoate, vigabatrin
-
-
?
(R)-4-amino-3-fluorobutanoic acid
4-aminobut-2-enoic acid + HF
-
-
-
?
(R,S)-4-amino-3-fluorobutanoic acid
4-aminobut-2-enoic acid + HF
neither enantiomer is a substrate for transamination. The rate of elimination of HF from the (R)-enantiomer is at least 10 times greater than that for the (S)-enantiomer
-
-
?
(S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid + 2-oxoglutarate
4-oxo-4,5-dihydro-2-thiophenecarboxylic acid + L-glutamate
-
mechanism-based inactivator that partly undergoes inactivation
-
-
?
1H-tetrazole-5-butanamine + 2-oxoglutarate
(1H-tetrazol-5-yl)-butyraldehyde + L-glutamate
-
-
-
-
?
1H-tetrazole-5-ethanamine + 2-oxoglutarate
(1H-tetrazol-5-yl)-acetaldehyd + L-glutamate
-
-
-
-
?
1H-tetrazole-5-propanamine + 2-oxoglutarate
(1H-tetrazol-5-yl)-propionaldehyde + L-glutamate
-
-
-
-
?
3-(aminomethyl)benzoic acid + 2-oxoglutarate
3-(iminomethyl)benzoic acid + L-glutamate
3.4% of the activity with 4-aminobutanoate
-
-
?
3-aminoisobutanoate + 2-oxoglutarate
L-glutamate + 3-oxoisobutanoate
3-aminopropanesulfonate + 2-oxoglutarate
3-sulfopropanal + L-glutamate
substrate is homotaurine
-
-
?
4-(aminomethyl)-1H-pyrrole-2-carboxylic acid + 2-oxoglutarate
?
-
-
-
-
?
4-(aminomethyl)furan-2-carboxylic acid + 2-oxoglutarate
?
-
-
-
-
?
4-(aminomethyl)furan-3-carboxylic acid + 2-oxoglutarate
?
-
-
-
-
?
4-(aminomethyl)thiophene-2-carboxylic acid + 2-oxoglutarate
?
-
-
-
-
?
4-(aminomethyl)thiophene-3-carboxylic acid + 2-oxoglutarate
?
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
4-aminobutanoate + pyruvate
4-oxobutanoate + alanine
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
4-aminobutyrate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
5-(aminomethyl)-1H-pyrrole-2-carboxylic acid + 2-oxoglutarate
?
-
-
-
-
?
5-(aminomethyl)furan-2-carboxylic acid + 2-oxoglutarate
?
-
-
-
-
?
5-(aminomethyl)thiophene-2-carboxylic acid + 2-oxoglutarate
?
-
-
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
5-aminovaleric acid + pyruvate
5-oxopentanoate + L-alanine
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
cadaverine + 2-oxoglutarate
L-glutamate + 5-aminopentanal
-
-
-
-
?
cadaverine + 2-oxoglutarate
L-glutamate + ?
-
poor amino donor
-
-
r
D-lysine + 2-oxoglutarate
L-glutamate + 5-aminopentanal
DL-3-amino-1-cyclopentene-1-carboxylic acid + 2-oxoglutarate
3-oxo-1-cyclopentene-1-carboxylic acid + L-glutamate
-
analogue of 4-aminobutanoate, vigabatrin
-
-
?
DL-3-hydroxy-4-aminobutanoate + 2-oxoglutarate
L-glutamate + 3-hydroxy-4-oxobutanoate
DL-ornithine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
gamma-aminobutyric acid
?
-
-
-
?
hypotaurine + 2-oxoglutarate
L-glutamate + 2-oxoethanesulfinic acid
-
poor amino donor
-
-
r
L-3-aminoisobutanoate + 2-oxoglutarate
?
-
-
-
-
?
L-lysine + 2-oxoglutarate
L-glutamate + (S)-2-amino-6-oxohexanoate
-
-
i.e. L-2-aminoadipate-6-semialdehyde
-
?
L-ornithine + 2-oxoglutarate
L-glutamate + (S)-2-amino-5-oxopentanoate
-
-
i.e. L-glutamate-gamma-semialdehyde
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
tetrazole-5-butanamine + 2-oxoglutarate
?
-
-
-
-
?
tetrazole-5-ethanamine + 2-oxoglutarate
?
-
-
-
-
?
tetrazole-5-propanamine + 2-oxoglutarate
?
-
-
-
-
?
[2-(aminomethyl)phenyl]acetic acid + 2-oxoglutarate
(2-formylphenyl)acetic acid + L-glutamate
5.65% of the activity with 4-aminobutanoate
-
-
?
[3-(aminomethyl)phenyl]acetic acid + 2-oxoglutarate
(3-formylphenyl)acetic acid + L-glutamate
0.78% of the activity with 4-aminobutanoate
-
-
?
additional information
?
-
3-aminoisobutanoate + 2-oxoglutarate
L-glutamate + 3-oxoisobutanoate
-
-
-
-
r
3-aminoisobutanoate + 2-oxoglutarate
L-glutamate + 3-oxoisobutanoate
-
transamination at 55% the rate of 4-aminobutanoate
-
-
r
3-aminoisobutanoate + 2-oxoglutarate
L-glutamate + 3-oxoisobutanoate
-
-
-
-
r
3-aminoisobutanoate + 2-oxoglutarate
L-glutamate + 3-oxoisobutanoate
-
transamination at 14% the rate of 4-aminobutanoate
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
Candida guilliermondii var. membranaefaciens
-
best substrate
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
Candida guilliermondii var. membranaefaciens Y43
-
best substrate
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
specific for 2-oxoglutarate
i.e. succinic semialdehyde + L-Glu
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
involved in gamma-aminobutyrate metabolism
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
no substrate: 2-oxoglutarate
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
no substrate: 2-oxoglutarate
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
best substrate at pH 9.5 as well as at pH 8.5
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
inducible enzyme
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
involved in 4-aminobutanoate metabolism via the GABA shunt pathway
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
involved in 4-aminobutanoate metabolism via the GABA shunt pathway
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
best substrate
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
involved in beta-alanine metabolism
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
native enzyme Atu3300 shows very low or no GABA transaminase activity
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
native enzyme Atu3300 shows very low or no GABA transaminase activity
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
native enzyme Atu3300 shows very low or no GABA transaminase activity
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
-
-
-
?
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
-
-
-
-
?
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
-
-
-
-
?
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
-
-
-
?
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
-
at 16% of the activity of 2-oxoglutarate
-
-
r
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
-
at 16% of the activity of 2-oxoglutarate
-
-
r
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
-
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + alanine
-
not using 2-oxoglutarate
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + alanine
-
not using 2-oxoglutarate
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + alanine
-
at 7% of the activity of 2-oxoglutarate
-
-
r
4-aminobutanoate + pyruvate
4-oxobutanoate + alanine
-
at 7% of the activity of 2-oxoglutarate
-
-
r
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
-
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
-
-
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
-
-
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
-
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
-
-
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
-
-
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
-
-
-
?
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
-
-
-
?
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
-
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
Candida guilliermondii var. membranaefaciens
-
transamination at 45% the rate of 4-aminobutanoate
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
Candida guilliermondii var. membranaefaciens Y43
-
transamination at 45% the rate of 4-aminobutanoate
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
-
-
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
-
transamination at 48% the rate of 4-aminobutanoate
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
-
transamination at 60% the rate of 4-aminobutanoate
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
-
-
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
-
transamination at 85% the rate of 4-aminobutanoate
-
-
?
5-aminovaleric acid + pyruvate
5-oxopentanoate + L-alanine
-
-
47.7% of the activity with 4-aminobutanoate
-
?
5-aminovaleric acid + pyruvate
5-oxopentanoate + L-alanine
-
-
47.7% of the activity with 4-aminobutanoate
-
?
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
Candida guilliermondii var. membranaefaciens
-
transamination at 27% the rate of 4-aminobutanoate
-
-
?
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
Candida guilliermondii var. membranaefaciens Y43
-
transamination at 27% the rate of 4-aminobutanoate
-
-
?
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
-
-
-
-
?
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
-
transamination at 29% the rate of 4-aminobutanoate
-
-
?
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
-
-
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
Candida guilliermondii var. membranaefaciens
-
poor substrate
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
Candida guilliermondii var. membranaefaciens Y43
-
poor substrate
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
effective amino group donor
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
effective amino group donor
-
-
r
D-lysine + 2-oxoglutarate
L-glutamate + 5-aminopentanal
-
poor amino donor
-
-
r
D-lysine + 2-oxoglutarate
L-glutamate + 5-aminopentanal
-
poor amino donor
-
-
r
DL-3-hydroxy-4-aminobutanoate + 2-oxoglutarate
L-glutamate + 3-hydroxy-4-oxobutanoate
-
-
-
-
r
DL-3-hydroxy-4-aminobutanoate + 2-oxoglutarate
L-glutamate + 3-hydroxy-4-oxobutanoate
-
-
-
-
r
DL-3-hydroxy-4-aminobutanoate + 2-oxoglutarate
L-glutamate + 3-hydroxy-4-oxobutanoate
-
transamination at 20% the rate of 4-aminobutanoate
-
-
r
DL-ornithine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
-
poor amino donor
-
-
?
DL-ornithine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
-
poor amino donor
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
reaction of EC 2.6.1.11
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
reaction of EC 2.6.1.19
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
reaction of EC 2.6.1.11
-
-
?
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
-
-
-
-
?
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
-
poor amino donor
-
-
r
additional information
?
-
cannot utilize 2-oxoglutarate as amino acceptor
-
-
?
additional information
?
-
-
cannot utilize 2-oxoglutarate as amino acceptor
-
-
?
additional information
?
-
-
cannot utilize 2-oxoglutarate as amino acceptor
-
-
?
additional information
?
-
-
cannot utilize 2-oxoglutarate as amino acceptor
-
-
?
additional information
?
-
Candida guilliermondii var. membranaefaciens
-
no substrates are L-aminovalerate, L-norleucine, straight alpha-amino acids, diamino acids
-
-
?
additional information
?
-
Candida guilliermondii var. membranaefaciens Y43
-
no substrates are L-aminovalerate, L-norleucine, straight alpha-amino acids, diamino acids
-
-
?
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected
-
-
-
additional information
?
-
-
does not use pyruvate as amino acceptor
-
-
?
additional information
?
-
does not use pyruvate as amino acceptor
-
-
?
additional information
?
-
does not use pyruvate as amino acceptor
-
-
?
additional information
?
-
-
overview
-
-
?
additional information
?
-
-
no amino acceptors are oxaloacetate, pyruvate
-
-
?
additional information
?
-
-
no amino acceptors are 2-oxobutyrate, phenylpyruvate, alpha-ketoadipate
-
-
?
additional information
?
-
-
no amino acceptors are oxaloacetate, pyruvate
-
-
?
additional information
?
-
(Pl)EctB also preferably catalyzes a EctB-type reaction, EC 2.6.1.76
-
-
-
additional information
?
-
(Pl)EctB also preferably catalyzes a EctB-type reaction, EC 2.6.1.76
-
-
-
additional information
?
-
-
enzyme is induced in cells grown on 4-guanidinobutyrate, 4-aminobutyrate, or putrescine as the only carbon and nitrogen source. GABAT functions in the biosynthesis of arginine by converting N2-acetyl-L-glutamate 5-semialdehyde to N2-acetyl-L-ornithine as well as in catabolic reactions during growth on putrescine or 4-guanidinobutyrate but not during growth on arginine
-
-
?
additional information
?
-
-
overview
-
-
?
additional information
?
-
-
no amino acceptors are oxaloacetate, pyruvate
-
-
?
additional information
?
-
-
no substrate: lysine
-
-
?
additional information
?
-
-
no amino acceptors are ketomalonic acid, alpha-ketoisovaleric acid
-
-
?
additional information
?
-
-
aspartate, L-2,4-diaminoglutarate, alanine, D-glutamate or malonic semialdehyde cannot replace L-glutamate or succinic semialdehyde in the reverse reaction
-
-
?
additional information
?
-
-
GABase activity against beta-alanine, epsilon-amino-n-caproic acid, L-ornithine, L-lysine, and L-aspartic acid is between 0.3 to 2.3% of the activity against 4-aminobutanoate
-
-
?
additional information
?
-
-
GABase activity against beta-alanine, epsilon-amino-n-caproic acid, L-ornithine, L-lysine, and L-aspartic acid is between 0.3 to 2.3% of the activity against 4-aminobutanoate
-
-
?
additional information
?
-
-
no substrates are taurine, 3-aminopropane sulfonate, glycine
-
-
?
additional information
?
-
-
no substrates are taurine, 3-aminopropane sulfonate, glycine
-
-
?
additional information
?
-
-
overview
-
-
?
additional information
?
-
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase activities
-
-
-
additional information
?
-
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase activities
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-aminopropanesulfonate + 2-oxoglutarate
3-sulfopropanal + L-glutamate
substrate is homotaurine
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
4-aminobutyrate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
additional information
?
-
-
enzyme is induced in cells grown on 4-guanidinobutyrate, 4-aminobutyrate, or putrescine as the only carbon and nitrogen source. GABAT functions in the biosynthesis of arginine by converting N2-acetyl-L-glutamate 5-semialdehyde to N2-acetyl-L-ornithine as well as in catabolic reactions during growth on putrescine or 4-guanidinobutyrate but not during growth on arginine
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
involved in gamma-aminobutyrate metabolism
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
inducible enzyme
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
involved in 4-aminobutanoate metabolism via the GABA shunt pathway
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
involved in 4-aminobutanoate metabolism via the GABA shunt pathway
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
involved in beta-alanine metabolism
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutanoate + pyruvate
succinate semialdehyde + L-alanine
-
-
-
r
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
-
-
-
?
4-aminobutyrate + 2-oxoglutarate
succinic semialdehyde + L-glutamate
-
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
reaction of EC 2.6.1.19
-
-
?
N2-acetyl-L-ornithine + 2-oxoglutarate
N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
reaction of EC 2.6.1.11
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(+/-)-(1S,2R,4S,5S)-4-amino-6,6-difluorobicyclo[3.1.0]hexane-2-carboxylic acid
-
10 mM, weak, reversible inhibitor
(+/-)-(1S,2S,4S,5S)-4-amino-6,6-difluorobicyclo[3.1.0]hexane-2-carboxylic acid
-
10 mM, weak, reversible inhibitor
(+/-)piperidine-3-sulfonic acid
-
-
(1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid
-
mechanism-based inactivation, adduct formed is derived from enamine mechanism
(1R,4S)-4-amino-2-cyclopentene-1-carboxylic acid
-
analogue of 4-aminobutanoate, vigabatrin
(1R,4S)-4-amino-3-fluorocyclopent-2-enecarboxylic acid
-
weak reversible inhibition in the presence of beta-mercaptoethanol
(1R,4S)-4-amino-3-pentafluoroethylcyclopent-2-enecarboxylic acid
-
weak reversible inhibition in the presence of beta-mercaptoethanol
(1R,4S)-4-amino-3-trifluoromethylcyclopent-2-enecarboxylic acid
-
irreversible inhibition in the presence of beta-mercaptoethanol
(1S,2S,3E)-2-amino-3-(fluoromethylidene)cyclopentanecarboxylic acid
monofluorinated analog of inhibitor CPP-115. Compound produces a metabolite that induces disruption of the Glu270-Arg445 salt bridge of GABA transaminase to accommodate interaction between the metabolite formyl group and Arg445. The inactivation mechanism is initiated by Schiff base formation with the active site pyridoxal 5'-phosphate, followed by gamma-proton removal
(1S,2S,3Z)-2-amino-3-(fluoromethylidene)cyclopentanecarboxylic acid
monofluorinated analog of inhibitor CPP-115. Compound produces a metabolite that induces disruption of the Glu270-Arg445 salt bridge of GABA transaminase to accommodate interaction between the metabolite formyl group and Arg445. The inactivation mechanism is initiated by Schiff base formation with the active site pyridoxal 5'-phosphate, followed by gamma-proton removal
(1S,3S)-(Z)-3-amino-4-(2,2,2-trifluoroethylidene)cyclopentanecarboxylic acid
-
inhibition in the presence of beta-mercaptoethanol
(1S,3S)-3-amino-4-(2,2,2-trifluoro-1-trifluoromethylethylidene)-cyclopentanecarboxylic acid
-
weak reversible inhibition in the presence of beta-mercaptoethanol
(1S,3S)-3-amino-4-difluoromethylenecyclopentanecarboxylic acid
-
potent irreversible inhibitor
(1S,3S)-3-amino-4-difluoromethylenyl-1-cyclopentanoic acid
(1S,4R)-4-amino-2-cyclopentene-1-carboxylic acid
-
analogue of 4-aminobutanoate, vigabatrin
(1S,4S)-2-(difluoromethylidene)-4-(1H-tetrazol-5-yl)cyclopentanamine
-
time-dependent inactivation, ratio kinact/KI value at pH 8.0 is 2.48 per min and mM
(2E)-4-methylpentan-2-one N-(2,4-dimethylphenyl)semicarbazone
-
57% inhibition at 0.125 mM
(2E)-butan-2-one N-(2,4-dimethylphenyl)semicarbazone
-
89% inhibition at 0.0625 mM
(4R)-4-amino-1-cyclopentene-1-carboxylic acid
-
analogue of 4-aminobutanoate, vigabatrin
(4S)-4-amino-1-cyclopentene-1-carboxylic acid
-
analogue of 4-aminobutanoate, vigabatrin
(R,S)-4-amino-3-fluorobutanoic acid
the (R)-enantiomer inhibits the transamination of gamma-aminobutanoic acid 10 times more effectively than the (S)-enantiomer. On binding of free 4-amino-3-fluorobutanoic acid to enzyme the optimal conformation places the C-NH3 + and C-F bonds gauche in the (R)-enantiomer but anti in the (S)-enantiomer
(S)-3-amino-4-(difluoromethylenyl)cyclopent-1-ene-1-carboxylic acid
(S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid
-
mechanism-based inactivator, reacts via aromatization mechanism
(Z)-4-amino-2-butenoic acid
-
-
1-(4-acetylphenyl)-3-(4-bromophenyloxy)-pyrrolidine-2,5-dione
-
1-(4-acetylphenyl)-3-(salicyldehydroxy)-pyrrolidine-2,5-dione
-
1H-tetrazole-5-(alpha-vinyl-propanamine)
-
-
2,4-dimethylphenyl semicarbazide hydrochloride
-
90% inhibition at 0.0625 mM
2-Aminobenzenesulfonate
-
-
2-aminobutanoate
Candida guilliermondii var. membranaefaciens
-
-
2-aminoethane phosphonic acid
-
-
2-N-(acetylamino)cyclohexane sulfonic acid
-
-
3-(aminomethyl)benzoic acid
poor competitive inhibitor
3-aminocyclohexanecarboxylic acid
-
10 mM
3-chloro-1-(4-hydroxyphenyl)propan-1-one
-
irreversible and potent inhibitor, about 30% residual activity at 0.06 mM, 2-oxoglutarate prevents the enzyme from inactivation
3-Chloro-4-aminobutanoate
-
-
3-Mercaptopropionic acid
-
-
3-Methyl-2-benzothiazolone hydrazone hydrochloride
-
-
3-Phenyl-4-aminobutanoate
-
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-ethylphenyl)butanamide
4-(1,3-dioxoisoindolin-2-yl)-N-(4-fluorophenyl)butanamide
4-(1,3-dioxoisoindolin-2-yl)-N-(4-iodophenyl)butanamide
4-(1,3-dioxoisoindolin-2-yl)-N-(4-methoxyphenyl)butanamide
4-(1,3-dioxoisoindolin-2-yl)-N-(4-nitrophenyl)butanamide
4-(1,3-dioxoisoindolin-2-yl)-N-p-tolylbutanamide
4-(1,3-dioxoisoindolin-2-yl)-N-phenylbutanamide
4-(aminomethyl)-1H-pyrrole-2-carboxylic acid
-
-
4-(aminomethyl)furan-2-carboxylic acid
-
-
4-(aminomethyl)furan-3-carboxylic acid
-
-
4-(aminomethyl)thiophene-2-carboxylic acid
-
-
4-(aminomethyl)thiophene-3-carboxylic acid
-
-
4-acryloylphenol
-
potent inhibitor
4-amino-2-fluorobutanoate
-
reversible, competitive to 4-aminobutanoate
4-amino-5-fluoropentanoic acid
-
potent irreversible inhibitor
4-Amino-hex-5-enoic acid
-
substrate analogue, irreversible, in vitro and in vivo
4-Aminohex-5-ynoic acid
-
irreversible, in vitro and in vivo, kinetics
4-ethynyl-4-aminobutanoate
-
4-hydroxybenzylamine
-
IC50: 0.0154 mM, competitive inhibition
5,5'-dithiobis-2-nitrobenzoic acid
-
95% loss of activity
5-(aminomethyl)-1H-pyrrole-2-carboxylic acid
-
-
5-(aminomethyl)furan-2-carboxylic acid
-
-
5-(aminomethyl)thiophene-2-carboxylic acid
-
-
5-amino-1,3-cyclohexadienylcarboxylate
-
5-Iodouracil
-
84% inhibition at 1 mM
6-Azauracil
-
63% inhibition at 1 mM, reversible by dialysis, not by pyridoxal phosphate addition
alpha-alanine
Candida guilliermondii var. membranaefaciens
-
-
Ba2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
Baclofen
-
injection of 0.01 mg/g body weight reduces GABA-T mRNA level 2fold; i.p. injection of sexually regressed female goldfish results in significant increase in serum luteinising hormone after 6 h. About 2fold decrease both in glutamic acid decarboxylase 67 and gamma-aminobutanoate transaminase mRNa in the hypothalamus
beta-cypermethrin
GABA transaminase activity detected is significantly decreased in the cerebral cortex of mice 2 h after beta-cypermethrin administration. beta-Cypermethrin (80 mg/kg) significantly increases GABA levels in the cerebral cortex of mice, at both 2 and 4 h after treatment, compared with the control. The number of positive granules is increased in the cerebral cortex of mice 4 h after exposure to 80 mg/kg beta-cypermethrin. No significant changes are found in glutamate decarboxylase activity, or the expression of GABA transaminase protein and GABAB receptors mRNA, in the cerebral cortex of mice, except that 80 mg/kg beta-cypermethrin causes a significant decrease in GABAA receptors mRNA expression 4 h after administration
Branched-chain fatty acids
-
Ca2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
Cd2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
cis-3-aminocyclohex-4-ene-1-carboxylic acid
-
conformationally rigid analogue of vigabatrin, mechanism
Co2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
cycloserine
-
90% inhibition at 1 mM
Divalent metal ions
-
with decreasing efficiency: Hg2+, Cd2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
-
DL-3-amino-1-cyclopentene-1-carboxylic acid
-
analogue of 4-aminobutanoate, vigabatrin
DL-trans-4-amino-2-cyclopentene-1-carboxylic acid
-
analogue of 4-aminobutanoate, vigabatrin
ethanolamine O-sulfate
-
active-site directed, ir, in vitro and in vivo, kinetics
ethylamine-2-sulfonic acid
-
i.e. taurine, competitive
falcarindiol
-
active-site directed, irreversible, 23% residual activity at 14 mM, isolate of root of Angelica dahurica
gamma-vinyl 4-aminobutanoate
-
0.1 mM, complete inhibition
gastrodigenin
-
30.87% inhibition at 0.01 mM
glycine
competitive inhibitor of pyruvate-dependent GABA-T activity
imperatorin
-
active-site directed, irreversible, 14% residual activity at 14 mM, isolate of root of Angelica dahurica
Lysyl reagents
-
2-oxoglutarate protects
-
Mg2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
Mn2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
N-(2,4-dichlorophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
N-(2,4-difluorophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
N-(4-bromophenyl)-3-(4-chlorophenyl)-6,7-dimethoxy-3a,4-dihydroindeno[1,2-c]pyrazole-2(3H)-carboxamide
molecular docking to propose the binding interaction with a three-dimensional structural model of the gamma-aminobutyric acid amino transferase. The compound successfully binds to the active pocket of the enzyme with good predicted affinities
N-(4-bromophenyl)-3-(4-fluorophenyl)-6,7-dimethoxy-3a,4-dihydroindeno[1,2-c]pyrazole-2(3H)-carboxamide
molecular docking to propose the binding interaction with a three-dimensional structural model of the gamma-aminobutyric acid amino transferase. The compound successfully binds to the active pocket of the enzyme with good predicted affinities
N-(4-bromophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
N-(4-chloro-2-iodophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
N-(4-chloro-2-methylphenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
N-(4-chlorophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
Ni2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
oleanolic acid
-
20.2% inhibition at 0.1 mg/ml
propan-2-one N-(2,4-dimethylphenyl)semicarbazone
-
44% inhibition at 0.25 mM
rosmarinic acid
-
40.2% inhibition at 0.1 mg/ml
S-vigabatrin
-
ratio kinact/KI is1.7 per min and mM at pH 8.5, 0.11per min and mM at pH 6.5, respectively
Sr2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
tetrazole-5-(alpha-vinyl-propanamine)
-
-
trimethylcitryl-beta-D-galactopyranoside
-
56.8% inhibition at 0.01 mM
ursolic acid
-
19.9% inhibition at 0.1 mg/ml
Valproic acid
-
65.4% inhibition at 0.01 mM
[2-(aminomethyl)phenyl]acetic acid
poor competitive inhibitor
[3-(aminomethyl)phenyl]acetic acid
poor competitive inhibitor
(1S,3S)-3-amino-4-difluoromethylenyl-1-cyclopentanoic acid
-
(1S,3S)-3-amino-4-difluoromethylenyl-1-cyclopentanoic acid
i.e. CPP-115, high inhibition of GABA-AT. Potential mechanism of inactivation of GABA-AT by CPP-115, overview. CPP-115 has been designed to inactivate GABA-AT via a Michael addition mechanism that would lead to a covalent adduct with the enzyme, similar to that with vigabatrin. But it is discovered from the crystal structure of GABAT inactivated by CPP-115 that the enzyme forms a noncovalent, tightly bound complex with CPP-115 via strong electrostatic interactions between the two carboxylate groups in the resulting metabolite with Arg192 and Arg445 in the active site. Inactivation is initiated by Schiff base formation between CPP-115 and the lysine-bound PLP, followed by gamma-proton removal and tautomerization, resulting in a highly reactive Michael acceptor. Before Lys329 can attack this Michael acceptor, catalytic hydrolysis of the difluoromethylenyl group occurs, leading to the PLP-bound dicarboxylate metabolite, which elicits a conformational change in the enzyme and tightly binds to Arg192 and Arg445 via electrostatic interactions. Molecular dynamic simulations and computer modeling indicate a movement of the difluoromethylenyl group of the Michael acceptor away from Lys329 upon enzyme-catalyzed tautomerization, leaving it too far away from Lys329 for nucleophilic attack. The enzyme catalyzes its hydrolysis instead
(1S,3S)-3-amino-4-difluoromethylenyl-1-cyclopentanoic acid
i.e. CPP-115, high inhibition of GABA-AT. Potential mechanism of inactivation of GABA-AT by CPP-115, overview. CPP-115 has been designed to inactivate GABA-AT via a Michael addition mechanism that would lead to a covalent adduct with the enzyme, similar to that with vigabatrin. But it is discovered from the crystal structure of GABAAT inactivated by CPP-115 that the enzyme forms a noncovalent, tightly bound complex with CPP-115 via strong electrostatic interactions between the two carboxylate groups in the resulting metabolite with Arg192 and Arg445 in the active site. Inactivation is initiated by Schiff base formation between CPP-115 and the lysine-bound PLP, followed by gamma-proton removal and tautomerization, resulting in a highly reactive Michael acceptor. Before Lys329 can attack this Michael acceptor, catalytic hydrolysis of the difluoromethylenyl group occurs, leading to the PLP-bound dicarboxylate metabolite, which elicits a conformational change in the enzyme and tightly binds to Arg192 and Arg445 via electrostatic interactions. Molecular dynamic simulations and computer modeling indicate a movement of the difluoromethylenyl group of the Michael acceptor away from Lys329 upon enzyme-catalyzed tautomerization, leaving it too far away from Lys329 for nucleophilic attack. The enzyme catalyzes its hydrolysis instead
(S)-3-amino-4-(difluoromethylenyl)cyclopent-1-ene-1-carboxylic acid
i.e. OV329, synthesis method, overview
(S)-3-amino-4-(difluoromethylenyl)cyclopent-1-ene-1-carboxylic acid
a highly potent gamma-aminobutyric acid aminotransferase inactivator for the treatment of addiction, design, synthesis method and mechanism, overview. Enzyme-bound structure analysis shows binding between the enzyme and a stable PLP-inhibitor noncovalent complex, rather than covalent modification, tautomeric forms of the structure of inhibitor-inactivated GABA-AT (eight theoretical tautomers of inhibitor-inactivated GABA-AT)
(S)-3-amino-4-(difluoromethylenyl)cyclopent-1-ene-1-carboxylic acid
a highly potent gamma-aminobutyric acid aminotransferase inactivator for the treatment of addiction, design, synthesis method and mechanism, overview. Enzyme-bound structure analysis shows binding between the enzyme and a stable PLP-inhibitor noncovalent complex, rather than covalent modification, tautomeric forms of the structure of inhibitor-inactivated GABA-AT (eight theoretical tautomers of inhibitor-inactivated GABA-AT)
2,4-diaminobutanoate
-
not
2,4-diaminobutanoate
-
kinetics
2,4-diaminobutanoate
-
not
2-oxoglutarate
Candida guilliermondii var. membranaefaciens
-
-
2-oxoglutarate
substrate inhibition
4-(1,3-dioxoisoindolin-2-yl)-N-(4-ethylphenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-ethylphenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-fluorophenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-fluorophenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-iodophenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-iodophenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-methoxyphenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-methoxyphenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-nitrophenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-(4-nitrophenyl)butanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-p-tolylbutanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-p-tolylbutanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-phenylbutanamide
-
4-(1,3-dioxoisoindolin-2-yl)-N-phenylbutanamide
-
4-aminohex-5-enoic acid
-
i.e. gamma-vinyl GABA, competitive, does not affect transamination process of 2-oxoglutarate
4-aminohex-5-enoic acid
-
-
4-hydroxybenzaldehyde
-
IC50: 0.0165 mM, competitive inhibition
4-hydroxybenzaldehyde
-
competitive inhibitor of GABA transaminase
4-hydroxybenzaldehyde
-
potent inhibitor
5-fluorouracil
-
weak
Aminooxyacetate
-
Aminooxyacetate
-
80% inhibition at 2 mM
Aminooxyacetate
-
99% inhibition at 1 mM
Aminooxyacetate
-
kinetics
beta-Alanine
competitive inhibitor of pyruvate-dependent GABA-T activity
beta-Alanine
Candida guilliermondii var. membranaefaciens
-
-
beta-Alanine
moderate inhibitor; moderate inhibitor
Branched-chain fatty acids
-
-
-
Branched-chain fatty acids
-
-
-
Butyric acid
Candida guilliermondii var. membranaefaciens
-
-
carbonyl reagents
-
-
-
Cu2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
D-cycloserine
-
-
D-penicillamine
-
-
ethanol
-
10% v/v, weak
ethanol
-
in presence of disulfiram, i.e. N,N,N,N-tetraethylthiuram disulfide
gabaculine
-
i.e. 5-amino-1,3-cyclohexadienylcarboxylate, ir, kinetics; not its tert-butylcarbamate derivative
gabaculine
-
80% inhibition at 2 mM
gabaculine
-
98% inhibition at 1 mM
gabaculine
-
IC50: 0.0018 mM, potent and irreversible inhibitor
gabaculine
-
highly specific GABAtransaminase inhibitor
HgCl2
-
strong, 50% inhibition at 0.007 mM
HgCl2
-
24% inhibition at 0.05 mM, pyridoxal 5'-phosphate protects
hydrazine
-
-
hydroxylamine
-
-
monoiodoacetate
-
not
Muscimol
-
injection of 0.001 mg/g body weight reduces GABA-T mRNA level 15fold; i.p. injection of sexually regressed female goldfish results in significant increase in serum luteinising hormone after 6 h. About 10fold decrease in glutamic acid decarboxylase 65 and 15fold in gamma-aminobutanoate transaminase mRNa in the hypothalamus
Muscimol
-
i.e. 5-(aminomethyl)-3-isoxazolol
Muscimol
-
i.e. 5-(aminomethyl)-3-isoxazolol
N-(2,4-dichlorophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(2,4-dichlorophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(2,4-difluorophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(2,4-difluorophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(4-bromophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(4-bromophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(4-chloro-2-iodophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(4-chloro-2-iodophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(4-chloro-2-methylphenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(4-chloro-2-methylphenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(4-chlorophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
N-(4-chlorophenyl)-4-(1,3-dioxoisoindolin-2-yl)butanamide
-
ornithine
competitive inhibitor of pyruvate-dependent GABA-T activity
ornithine
moderate inhibitor; moderate inhibitor
p-chloromercuribenzoate
-
strong
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
phenylhydrazine
-
-
propionic acid
Candida guilliermondii var. membranaefaciens
-
-
SH-group reagents
-
-
-
SH-group reagents
-
2-mercaptoethanol or DTT reactivates
-
SH-group reagents
-
2-oxoglutarate protects
-
Succinic semialdehyde
-
-
Succinic semialdehyde
-
substrate inhibition
vigabatrin
competitive inhibitor of pyruvate-dependent GABA-T activity
vigabatrin
-
complete inhibition at 0.5 mM
vigabatrin
-
triggers a massive synaptic plasticity in retinal areas showing a normal layering of the retina shown by the withdrawal of rod but not cone photoreceptor terminals from the outer plexiform layers towards their cell bodies. Both rod bipolar cells and horizontal cells exhibit dendritic sprouting into the photoreceptor nuclear layer. Withdrawing rod photoreceptors appear to form ectopic contacts with growing postsynaptic dendrites. Neuronal plasticity is highly suggestive of an impaired glutamate release by photoreceptors
vigabatrin
-
gamma-vinyl GABA, anticonvulsant, induces spontaneous release of 4-aminobutanoate
vigabatrin
-
IC50: 0.35 mM
vigabatrin
-
chronical administration via drinking water at 30 and 81 mg per kg and day. Vigabatrin completely and reversibly eliminates the psychophysical evidence of tinnitus at both doses
vigabatrin
FDA-approved drug, inactivator of GABA-AT, moderate activity
vigabatrin
FDA-approved drug, inactivator of GABA-AT, moderate activity
additional information
no substrate inhibition: 4-aminobutanoate
-
additional information
-
no substrate inhibition: 4-aminobutanoate
-
additional information
a series of gamma-aminobutyric acid (GABA) derivatives obtained from 4-(1,3-dioxoisoindolin-2-yl)butanoic acid are synthesized and analyzed as inhibitory ligands docking against human ABAT as well as pig ABAT receptors. Active site docking study, overview
-
additional information
-
no inhibition by 6-azauridine, 6-azauridine 5'-phosphate, uracil, (iso)orotic acid, cytosine, thymine, dihydrothymine, 2-thiocytosine, thiourea; not inhibitory: 5-aminouracil
-
additional information
-
-
-
additional information
-
no inhibition by chelating agents, non-substrate L- or D-amino acids, metal ions
-
additional information
-
the methanol extract from Melissa officinalis is a potent in vitro inhibitor of GABA-T with IC50 of 0.55 mg/ml, inhibition decreases in the order: methanol extract, water extract, ethyl acetate extract and hexane extract (not inhibitory)
-
additional information
molecular dynamics simulations, design of mechanism-based inhibitors, drug design, overview
-
additional information
-
no inhibition by 3-aminopropane-1-sulfonic acid, isoguvacine (i.e. 1,2,3,4-tetrahydro-1-methyl-3-pyridine carboxylic acid), baclofen (i.e. beta-(aminomethyl)-4-chlorobenzenepropanoic acid), bicuculline, picrotoxin, Schistocerca gregaria: antiserum against sheep enzyme
-
additional information
-
no inhibition by chelating agents, non-substrate L- or D-amino acids, metal ions
-
additional information
-
(+/-)-(1S,3S,4S)-3-amino-4-fluorocyclohexanecarboxylic acid and (cis)-3-amino-5,5-difluorocylcohexanecarboxylic acid are no an inhibitors of GABA-AT at a concentration of 10 mM
-
additional information
a series of gamma-aminobutyric acid (GABA) derivatives obtained from 4-(1,3-dioxoisoindolin-2-yl)butanoic acid are synthesized and analyzed as inhibitory ligands docking against human ABAT as well as pig ABAT receptors. Active site docking study, overview
-
additional information
molecular dynamics simulations, design of mechanism-based inhibitors, drug design, overview
-
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0.0183
isoform GABA-T2, using pyruvate as amino cceptor
0.0209
isoform GABA-T2, using glyoxylate as amino cceptor
0.03
NCgl2515 activity, with substrate 4-aminobutanoate, pH 8.0, 30°C
0.1
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30°C
0.13
substrate beta-alanine, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30°C
0.14
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30°C
0.15
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30°C
0.1785
isoform GABA-T3, using glyoxylate as amino acceptor
0.2065
isoform GABA-T3, using pyruvate as amino acceptor
0.75
substrate gamma-aminobutanoate, continuous assay with succinate dehydrogenase, pH 8.0, 30°C
1.34
GABA-T activity, with substrate 4-aminobutanoate, pH 7.8, 30°C
1.6
substrate gamma-aminobutanoate, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30°C
170
-
pH 7.3, 37°C, liver enzyme
260
-
pH 7.3, 37°C, kidney enzyme
3.495
isoform GABA-T1, using glyoxylate as amino acceptor
3.52
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30°C
3.6
substrate gamma-aminobutanoate, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30°C
3.67
continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30°C
4.5
substrate beta-alanine, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30°C
5.79
isoform GABA-T1, using pyruvate as amino acceptor
52.33
Candida guilliermondii var. membranaefaciens
-
-
600
-
pH 7.3, 37°C, brain enzyme
12.8
using 4-aminobutanoate as substrate
12.8
substrate gamma-aminobutanoate, continuous assay with succinate dehydrogenase, pH 8.0, 30°C
4.9
-
-
additional information
specific activity is 52% with oxaloacetate as amino group acceptor (normalized to that with 2-oxoglutarate (100%: 46 mkat/kg protein)), the donor is homotaurine
additional information
-
specific activity is 52% with oxaloacetate as amino group acceptor (normalized to that with 2-oxoglutarate (100%: 46 mkat/kg protein)), the donor is homotaurine
additional information
specific activity is 59% with glyoxalate as amino group acceptor (normalized to that with 2-oxoglutarate (100%: 46 mkat/kg protein)), the donor is homotaurine
additional information
-
specific activity is 59% with glyoxalate as amino group acceptor (normalized to that with 2-oxoglutarate (100%: 46 mkat/kg protein)), the donor is homotaurine
additional information
specific activity is 63% with pyruvate as amino group acceptor (normalized to that with 2-oxoglutarate (100%: 46 mkat/kg protein)), the donor is homotaurine
additional information
-
specific activity is 63% with pyruvate as amino group acceptor (normalized to that with 2-oxoglutarate (100%: 46 mkat/kg protein)), the donor is homotaurine
additional information
specific activity is 9% with 2-oxobutyrate as amino group acceptor (normalized to that with 2-oxoglutarate (100%: 46 mkat/kg protein)), the donor is homotaurine
additional information
-
specific activity is 9% with 2-oxobutyrate as amino group acceptor (normalized to that with 2-oxoglutarate (100%: 46 mkat/kg protein)), the donor is homotaurine
additional information
specific activity of 0.02 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is homotaurine
additional information
-
specific activity of 0.02 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is homotaurine
additional information
specific activity of 0.03 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is 4-aminobutyrate
additional information
-
specific activity of 0.03 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with ammonium as the sole nitrogen source, substrate is 4-aminobutyrate
additional information
specific activity of 6.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is homotaurine
additional information
-
specific activity of 6.5 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is homotaurine
additional information
specific activity of 8.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinate semialdehyde
additional information
-
specific activity of 8.0 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is succinate semialdehyde
additional information
specific activity of 8.2 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is 4-aminobutyrate
additional information
-
specific activity of 8.2 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with 4-aminobutyrate as the sole nitrogen source, substrate is 4-aminobutyrate
additional information
specific activity of 8.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is homotaurine
additional information
-
specific activity of 8.3 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is homotaurine
additional information
specific activity of 9.9 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is 4-aminobutyrate
additional information
-
specific activity of 9.9 mkat/kg protein is detected in crude cell extracts of Cupriavidus necator grown with homotaurine as the sole nitrogen source, substrate is 4-aminobutyrate
additional information
specific activity with 3-aminopropanoate, taurine, (S)-cysteate, 3-aminopropanol or 4-aminobutanol as substrates is not detected
additional information
-
specific activity with 3-aminopropanoate, taurine, (S)-cysteate, 3-aminopropanol or 4-aminobutanol as substrates is not detected
additional information
specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 226% with 5-aminovalerate 6-aminocapronate as substrate
additional information
-
specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 226% with 5-aminovalerate 6-aminocapronate as substrate
additional information
specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 25% with 6-aminocapronate as substrate
additional information
-
specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 25% with 6-aminocapronate as substrate
additional information
specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 270% with 4-aminobutyrate as substrate
additional information
-
specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 270% with 4-aminobutyrate as substrate
additional information
-
stable-isotope dilution assay
additional information
-
3.4 units/mg in crude brain homogenate and 51.2 units/mg after 15fold purification
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evolution
EctB-type proteins are highly conserved
evolution
enzyme Atu3300 is predicted by Pfam to include an Aminotrans_3 (aminotransferase class-III) domain, which is characteristic of aminotransferases
evolution
transaminases structure comparisons, overview
evolution
-
transaminases structure comparisons, overview
-
evolution
-
transaminases structure comparisons, overview
-
evolution
-
EctB-type proteins are highly conserved
-
evolution
-
transaminases structure comparisons, overview
-
evolution
-
transaminases structure comparisons, overview
-
evolution
-
transaminases structure comparisons, overview
-
evolution
-
enzyme Atu3300 is predicted by Pfam to include an Aminotrans_3 (aminotransferase class-III) domain, which is characteristic of aminotransferases
-
evolution
-
enzyme Atu3300 is predicted by Pfam to include an Aminotrans_3 (aminotransferase class-III) domain, which is characteristic of aminotransferases
-
evolution
-
transaminases structure comparisons, overview
-
malfunction
-
patients with GABA-T deficiency show severe, nonspecific neurological manifestations, including psychomotor retardation, epilepsy, hypotonia, and hyperreflexia
malfunction
-
constitutive overexpression lines of GABA-T are generated in Arabidopsis. Brief cold treatments increases leaf GABA concentrations in both the WT and transgenic line OX1, but the concentrations in OX1 is consistently lower. These findings confirm that GABA-T limits the catabolism of GABA when its production is stimulated by stress, and suggest a bioengineering strategy for improving the availability of succinate semialdehyde for the Krebs cycle or GLYR1, a potential redox-modulating reaction during stress
malfunction
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT NCgl2515-deleted GAD strain remains unaltered when pH is maintained at pH 7.5-7.8, demonstrating that GABA decomposition is reduced
malfunction
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
malfunction
IncRNAs play an important role in the regulation of gene expression. Differential expression of lncRNAs (DELs) and mRNAs (DEMs) in myelodysplastic syndrome (MDS), profiling to construct a 4-aminobutyrate aminotransferase (ABAT)-DEL-DEM coexpression network in MDS development using the GO and KEGG pathway and network analyses. Compared with controls, there are 543 DELs and 2705 DEMs in MDS patients, among which 285 (52.5%) DELs are downregulated and 258 (47.5%) DELs are upregulated, whereas 1521 (56.2%) DEMs are downregulated and 1184 (43.70%) DEMs are upregulated in MDS patients. The ABAT-DEL-DEM coexpression network contains six DELs that are coexpressed with ABAT in MDS
malfunction
inhibition of GABA aminotransferase (GABA-AT), the enzyme that degrades GABA, is a possible strategy for the treatment of substance abuse. The raised GABA levels that occur as a consequence of the inhibition antagonize the rapid release of dopamine in the ventral striatum (nucleus accumbens) that follows an acute challenge by an addictive substance. In addition, increased GABA levels are also known to elicit an anticonvulsant effect in patients with epilepsy
malfunction
inhibition of GABA aminotransferase (GABA-AT), the enzyme that degrades GABA, is a possible strategy for the treatment of substance abuse. The raised GABA levels that occur as a consequence of the inhibition antagonize the rapid release of dopamine in the ventral striatum (nucleus accumbens) that follows an acute challenge by an addictive substance. In addition, increased GABA levels are also known to elicit an anticonvulsant effect in patients with epilepsy
malfunction
inhibition of GABAT is known to boost GABA concentration in the brain and thereby alleviates spasticity. Therefore, attenuating GABAT activity and enhancing GABA expression are a promising way to relieve spasticity following stroke. Waggle needling attenuates gamma-aminobutyric acid transaminase expression in the injured brain of rats with post-stroke spasticity comparable to the effect of baclofen
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT NCgl2515-deleted GAD strain remains unaltered when pH is maintained at pH 7.5-7.8, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT NCgl2515-deleted GAD strain remains unaltered when pH is maintained at pH 7.5-7.8, demonstrating that GABA decomposition is reduced
-
malfunction
-
inhibition of GABAT is known to boost GABA concentration in the brain and thereby alleviates spasticity. Therefore, attenuating GABAT activity and enhancing GABA expression are a promising way to relieve spasticity following stroke. Waggle needling attenuates gamma-aminobutyric acid transaminase expression in the injured brain of rats with post-stroke spasticity comparable to the effect of baclofen
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT NCgl2515-deleted GAD strain remains unaltered when pH is maintained at pH 7.5-7.8, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT NCgl2515-deleted GAD strain remains unaltered when pH is maintained at pH 7.5-7.8, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT NCgl2515-deleted GAD strain remains unaltered when pH is maintained at pH 7.5-7.8, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT NCgl2515-deleted GAD strain remains unaltered when pH is maintained at pH 7.5-7.8, demonstrating that GABA decomposition is reduced
-
metabolism
GABA metabolism
metabolism
GABA transaminase (GABAT) is the key catabolic enzyme of GABA metabolism
metabolism
in cyanobacteria 2-oxoglutarate dehydrogenase (2-OGDH) is missing. A bypass route via succinic semialdehyde (SSA), which utilizes 2-oxoglutarate decarboxylase (OgdA) and succinic semialdehyde dehydrogenase (SsaD) to convert 2-oxoglutarate (2-OG) into succinate, is identified, thus completing the TCA cycle in most cyanobacteria. In addition to the glyoxylate shunt that occurs in a few of cyanobacteria, the existence of a third variant of the TCA cycle connects these metabolites. The gamma-aminobutyric acid (GABA) shunt, is considered to be ambiguous because the GABA aminotransferase is missing in many cyanobacteria. N-acetylornithine aminotransferase (ArgD) can function as a GABA aminotransferase and, together with glutamate decarboxylase (GadA), it can complete a functional GABA shunt. Metabolite profiling of seven Synechococcus sp. PCC 7002 mutant strains related to these two routes to succinate proves the functional connectivity
metabolism
in cyanobacteria 2-oxoglutarate dehydrogenase (2-OGDH) is missing. A bypass route via succinic semialdehyde (SSA), which utilizes 2-oxoglutarate decarboxylase (OgdA) and succinic semialdehyde dehydrogenase (SsaD) to convert 2-oxoglutarate (2-OG) into succinate, is identified, thus completing the TCA cycle in most cyanobacteria. In addition to the glyoxylate shunt that occurs in a few of cyanobacteria, the existence of a third variant of the TCA cycle connects these metabolites. The gamma-aminobutyric acid (GABA) shunt, is considered to be ambiguous because the GABA aminotransferase is missing in many cyanobacteria. N-acetylornithine aminotransferase (ArgD) can function as a GABA aminotransferase and, together with glutamate decarboxylase (GadA), it can complete a functional GABA shunt. Metabolite profiling of seven Synechococcus sp. PCC 7002 mutant strains related to these two routes to succinate proves the functional connectivity
metabolism
the enzyme takes part in the GABA shunt pathway and GABA uptake/assimilation pathway in Corynebacterium glutamicum
metabolism
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH) GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
metabolism
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
the enzyme takes part in the GABA shunt pathway and GABA uptake/assimilation pathway in Corynebacterium glutamicum
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH) GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
the enzyme takes part in the GABA shunt pathway and GABA uptake/assimilation pathway in Corynebacterium glutamicum
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH) GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
GABA transaminase (GABAT) is the key catabolic enzyme of GABA metabolism
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
the enzyme takes part in the GABA shunt pathway and GABA uptake/assimilation pathway in Corynebacterium glutamicum
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH) GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
the enzyme takes part in the GABA shunt pathway and GABA uptake/assimilation pathway in Corynebacterium glutamicum
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH) GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
the enzyme takes part in the GABA shunt pathway and GABA uptake/assimilation pathway in Corynebacterium glutamicum
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH) GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
the enzyme takes part in the GABA shunt pathway and GABA uptake/assimilation pathway in Corynebacterium glutamicum
-
metabolism
-
unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH) GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
physiological function
-
GABA-T acts in salt responses in linking N and C metabolisms in roots, GABA-T is the most responsive step of GABA metabolism upon NaCl stress
physiological function
isoform GABA-T1 plays the predominant role in GABA metabolism in vegetative tissue
physiological function
Arabidopsis thaliana GABA-T functionally complements a Saccharomyces cerevisiae Uga1 mutant lacking GABA transaminase activity, despite mitochondrial localization of the Arabidopsis thaliana enzyme and cytosolic localization of the yeast enzyme. Recombinant GABA-T rescues mutant yeast's GABA growth defect, thermosensitivity and limiting production of reactive oxygen species, but GABA-T is about half as efficient in doing so Saccharomyces cerevisiae Uga1 gene product
physiological function
-
loss of GABA transaminase increases sleep, and affects metabolism such that flies lacking GABA transaminase fail to survive on carbohydrate media. GABA degradation product glutamate, rather than succinic semialdehyde, accounts for the metabolic phenotype of the mutants. Inhibition of GABA transaminase affects energetic pathways. Mutants display a general disruption in bioenergetics. The effects of GABA transaminase on sleep do not depend upon glutamate, indicating that GABAT regulates metabolic and sleep homeostasis through independent mechanisms
physiological function
mutations in the enzyme cause an autosomal recessive neurometabolic disorder and mitochondrial DNA depletion syndrome (MDS). ABAT functions in the mitochondrial nucleoside salvage pathway to facilitate conversion of dNDPs to dNTPs. Inhibition of ABAT by Vigabatrin causes depletion of mtDNA in photoreceptor cells that is prevented through addition of dNTPs in cell culture media
physiological function
GabT activity of the recombinant Escherichia coli enzyme expressed in Agrobacterium tumefaciens enhances the T-DNA transfer ability of Agrobacterium tumefaciens
physiological function
gamma-aminobutyric acid (GABA) is one of the chief inhibitory neurotransmitters in the central nerve system (CNS), plays pre- or postsynaptic inhibitory effects. GABA transaminase (GABAT) is the key catabolic enzyme of GABA metabolism. The modulation of GABA and its metabolism by acupuncture, particularly waggle needling, might attenuate GABAT and enhance GABA, alleviating post-stroke spasticity
physiological function
gamma-aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the central nervous system. The enzyme GABA aminotransferase (GABA-AT) degrades GABA
physiological function
gamma-aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the central nervous system. The enzyme GABA aminotransferase (GABA-AT) degrades GABA
physiological function
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase activities. N-acetylornithine aminotransferase (ArgD) can function as a GABA aminotransferase and, together with glutamate decarboxylase (GadA), it can complete a functional GABA shunt, metabolic profiling of glutamate decarboxylase expression strains
physiological function
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase activities. N-acetylornithine aminotransferase (ArgD) can function as a GABA aminotransferase and, together with glutamate decarboxylase (GadA, from Synechococcus sp. strain 6803) which is recombinantly expressed in strain Synechococcus sp. 7002, it can complete a functional GABA shunt, metabolic profiling of glutamate decarboxylase expression strains
physiological function
the Agrobacterium tumefaciens ability to mediate inter-kingdom DNA transfer in plant genetic engineering is inhibited by gamm-aminobutyric acid (GABA)
physiological function
production of glutaric acid depends on the expression of native gabT (EC 2.6.1.48) and gabD of Corynebacterium glutamicum, or on heterologous expression of davT (EC 2.6.1.48) and davD (EC 1.2.1.20) from Pseudomonas putida encoding 5-aminovalerate aminotransferase, and glutarate semialdehyde, respectively
physiological function
-
gamma-aminobutyric acid (GABA) is one of the chief inhibitory neurotransmitters in the central nerve system (CNS), plays pre- or postsynaptic inhibitory effects. GABA transaminase (GABAT) is the key catabolic enzyme of GABA metabolism. The modulation of GABA and its metabolism by acupuncture, particularly waggle needling, might attenuate GABAT and enhance GABA, alleviating post-stroke spasticity
-
additional information
active site structure analysis, the epsilon-amino group of Lys288, the catalytic residue of CgGABA-AT, may form an internal aldimine with the aldehydic carbon of PLP, which is required for catalysis
additional information
-
active site structure analysis, the epsilon-amino group of Lys288, the catalytic residue of CgGABA-AT, may form an internal aldimine with the aldehydic carbon of PLP, which is required for catalysis
additional information
bioinformatic analysis of lncRNAs correlated to enzyme ABAT
additional information
homology structure modeling using pig ABAT as template (PDB ID 6B6G)
additional information
homology structure modeling using pig ABAT as template (PDB ID 6B6G)
additional information
structural homology modeling of (Pl)EctB usimg the crystal structure of the GABA transaminase from Arthrobacter aurescens (PDB ID 4ATP, EC 2.6.1.19) as template
additional information
-
active site structure analysis, the epsilon-amino group of Lys288, the catalytic residue of CgGABA-AT, may form an internal aldimine with the aldehydic carbon of PLP, which is required for catalysis
-
additional information
-
active site structure analysis, the epsilon-amino group of Lys288, the catalytic residue of CgGABA-AT, may form an internal aldimine with the aldehydic carbon of PLP, which is required for catalysis
-
additional information
-
structural homology modeling of (Pl)EctB usimg the crystal structure of the GABA transaminase from Arthrobacter aurescens (PDB ID 4ATP, EC 2.6.1.19) as template
-
additional information
-
active site structure analysis, the epsilon-amino group of Lys288, the catalytic residue of CgGABA-AT, may form an internal aldimine with the aldehydic carbon of PLP, which is required for catalysis
-
additional information
-
active site structure analysis, the epsilon-amino group of Lys288, the catalytic residue of CgGABA-AT, may form an internal aldimine with the aldehydic carbon of PLP, which is required for catalysis
-
additional information
-
active site structure analysis, the epsilon-amino group of Lys288, the catalytic residue of CgGABA-AT, may form an internal aldimine with the aldehydic carbon of PLP, which is required for catalysis
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additional information
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active site structure analysis, the epsilon-amino group of Lys288, the catalytic residue of CgGABA-AT, may form an internal aldimine with the aldehydic carbon of PLP, which is required for catalysis
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E211S
crystallization data, decrease in kcat, decrease in Km-value for 2-oxoglutarate
E211S/I50G
drastic decrease in kcat-value
E211S/I50G/C77K
10fold increase in decarboxylation activity
E211S/I50G/C77R
drastic decrease in kcat-value
E211S/I50H/V80D
10fold increase in decarboxylation activity, change of reaction specificity to that of a decarboxylase
E211S/I50H/V80T
decrease in kcat, decrease in Km-value for 2-oxoglutarate
E211S/I50N/V80D
drastic decrease in kcat-value
E211S/I50N/V80T
drastic decrease in kcat-value
E211S/I50Q/G295Y/V241A
drastic decrease in kcat-value
I50Q
crystallization data, decrease in kcat, increase in Km-values
I50Q/G295Y
decrease in kcat, decrease in Km-value for 2-oxoglutarate
V241A
crystallization data, decrease in kcat, decrease in Km-value for 2-oxoglutarate
C321M
-
no enzymic activity, behaves as monomer even in absence of 2-mercaptoethanol
C321S
-
no enzymic activity, behaves as monomer even in absence of 2-mercaptoethanol
K357A
-
no enzymic activity, even not by addition of exogenous pyridoxal 5-phosphate
K357B
-
no enzymic activity, even not by addition of exogenous pyridoxal 5-phosphate
K357N
-
no enzymic activity, even not by addition of exogenous pyridoxal 5-phosphate
K357Q
-
no enzymic activity, even not by addition of exogenous pyridoxal 5-phosphate
L211F
homozygous missense mutation idientified in in a family with encephalomyopathic mitochondrial DNA depletion syndrome
K274A
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
K274H
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein
K274R
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
K274A
-
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
-
K274R
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site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
-
K330R
-
no catalytic activity, no pyridoxal 5'-phosphate covalently linked to protein
synthesis
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simultaneous expression of gamma-aminobutyric acid aminotransferase gabT and succinic semialdehyde dehydrogenase gabD genes in Escherichia coli. The mixture of both enzymes, called GABase, is the key enzyme for the enzymatic analysis of GABA
synthesis
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simultaneous expression of gamma-aminobutyric acid aminotransferase gabT and succinic semialdehyde dehydrogenase gabD genes in Escherichia coli. The mixture of both enzymes, called GABase, is the key enzyme for the enzymatic analysis of GABA
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additional information
Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
additional information
Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
additional information
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Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
additional information
-
Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
-
additional information
-
Agrobacterium tumefaciens is used to mediate inter-kingdom DNA transfer in plant genetic engineering. Gamma-aminobutyric acid (GABA) is a negative factor in the Agrobacterium-plant interaction, because it inhibits the DNA transfer. Generation of an Agrobacterium tumefaciens strain expressing the Escherichia coli gene gabT, which introduces GABA transaminase activity and the ability to degrade GABA, is achieved to circumvent the inhibitory effect of GABA. GabT activity enhances the T-DNA transfer ability of Agrobacterium tumefaciens
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additional information
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mutants of GABA transaminase suppress the severe phenotype of succinic semialdehyde dehydrogenase mutants in Arabidopsis
additional information
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the GABA transaminase loss-of-function mutant pop2-1 is oversensitive to ionic stress but not to osmotic stress
additional information
construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
additional information
construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
additional information
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
additional information
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
additional information
metabolic engineering of Corynebacterium glutamicum for the production of glutaric acid, a C5 dicarboxylic acid platform chemical, by co-expression of Pseudomonas putida davT, davB, and davD genes encoding lysine 2-monooxygenase, delta-aminovaleramidase, and glutarate semialdehyde dehydrogenase, respectively, in Corynebacterium glutamicum. Method optimization and evaluation. The glutaric acid biosynthesis pathway constructed in recombinant Corynebacterium glutamicum is engineered by examining strong synthetic promoters H30 and H36, Corynebacterium glutamicum codon-optimized davTDBA genes, and modification of davB gene with an N-terminal His6-tag to improve the production of glutaric acid. The use of N-terminal His6-tagged DavB is most suitable for the production of glutaric acid from glucose. Fed-batch fermentation on of the final engineered Corynebacterium glutamicum H30_GAHis strain, expressing davTDA genes along with davB fused with His6-tag at N-terminus can produce 24.5 g/l of glutaric acid with low accumulation of L-lysine (1.7 g/l), wherein 5-aminovaleric acid (5-AVA) ccumulation is not observed during fermentation. Metabolically engineered Corynebacterium glutamicum strain KCTC H30_GA-2 (engineered strain KCTC 1857) is able for catalysis of the biosynthesis of glutaric acid from glucose. Method optimization and evaluation, overview
additional information
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construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
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additional information
-
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
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construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain
-
additional information
-
C-terminal mutant lacking 5 amino acids, no interference with kinetical parameters or functional properties but change in stability of dimeric structure at acidic pH
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