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Information on EC 2.6.1.19 - 4-aminobutyrate-2-oxoglutarate transaminase
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EC Tree
2.6.1.19 4-aminobutyrate-2-oxoglutarate transaminaseIUBMB Comments
Requires pyridoxal phosphate. Some preparations also act on beta-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate.
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Word Map
- 2.6.1.19
- decarboxylase
-
gabaergic
- seizure
-
neurotransmitter
- epilepsy
- cortex
-
anticonvulsant
-
antiepileptic
- agonist
-
gamma-vinyl
-
aminooxyacetic
- bicuculline
- gabaculine
-
neurotransmission
- muscimol
-
shunt
- pyridoxal
- dopamine
- convulsion
-
gabab
- striatum
- benzodiazepine
- valproate
- hypothalamus
-
gamma-acetylenic
- baclofen
-
substantia
- diazepam
-
picrotoxin
-
transmitter
-
gaba-mediated
-
3hgaba
-
tiagabine
- ssadh
-
electroshock
-
enzyme-activated
-
nipecotic
- gabapentin
-
4.1.1.15
-
pentylenetetrazol
-
plp-dependent
-
kindling
- gamma-hydroxybutyrate
-
3-mercaptopropionic
-
gaba-induced
- homocarnosine
-
enamine
-
silverman
-
clonic
- medicine
-
ethosuximide
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
4-aminobutyrate aminotransferase, 4-aminobutyrate-2-ketoglutarate aminotransferase, 4-aminobutyrate-2-oxoglutarate aminotransferase, 4-aminobutyrate-2-oxoglutarate transaminase, 4-aminobutyric acid 2-ketoglutaric acid aminotransferase, 4-aminobutyric acid aminotransferase, ABAT, aminobutyrate aminotransferase, aminobutyrate transaminase, aminotransferase, aminobutyrate, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-aminobutyrate aminotransferase
4-aminobutyrate-2-ketoglutarate aminotransferase
-
-
-
-
4-aminobutyrate-2-oxoglutarate aminotransferase
-
-
-
-
4-aminobutyrate-2-oxoglutarate transaminase
-
-
-
-
4-aminobutyric acid 2-ketoglutaric acid aminotransferase
-
-
-
-
4-aminobutyric acid aminotransferase
-
-
-
-
aminobutyrate aminotransferase
-
-
-
-
aminobutyrate transaminase
aminotransferase, aminobutyrate
-
-
-
-
beta-alanine aminotransferase
-
-
-
-
beta-alanine transaminase
-
-
-
-
beta-alanine-oxoglutarate aminotransferase
-
-
-
-
beta-alanine-oxoglutarate transaminase
-
-
-
-
GABA aminotransferase
GABA transaminase
GABA transferase
-
-
-
-
GABA-2-oxoglutarate aminotransferase
-
-
-
-
GABA-2-oxoglutarate transaminase
-
-
-
-
GABA-alpha-ketoglutarate aminotransferase
-
-
-
-
GABA-alpha-ketoglutarate transaminase
-
-
-
-
GABA-alpha-ketoglutaric acid transaminase
-
-
-
-
GABA-alpha-oxoglutarate aminotransferase
-
-
-
-
GABA-oxoglutarate aminotransferase
-
-
-
-
GABA-oxoglutarate transaminase
-
-
-
-
GABA-T
gamma-aminobutyrate aminotransaminase
-
-
-
-
gamma-aminobutyrate transaminase
gamma-aminobutyrate-alpha-ketoglutarate aminotransferase
-
-
-
-
gamma-aminobutyrate-alpha-ketoglutarate transaminase
-
-
-
-
gamma-aminobutyrate:alpha-oxoglutarate aminotransferase
-
-
-
-
gamma-aminobutyric acid aminotransferase
gamma-aminobutyric acid pyruvate transaminase
-
-
-
-
gamma-aminobutyric acid transaminase
gamma-aminobutyric acid-2-oxoglutarate transaminase
-
-
-
-
gamma-aminobutyric acid-alpha-ketoglutarate transaminase
-
-
-
-
gamma-aminobutyric acid-alpha-ketoglutaric acid aminotransferase
-
-
-
-
gamma-aminobutyric transaminase
-
-
-
-
glutamate-succinic semialdehyde transaminase
-
-
-
-
Pop2
4-aminobutyrate aminotransferase
-
-
-
-
aminobutyrate transaminase
-
-
-
-
GABA aminotransferase
-
-
-
-
GABA transaminase
-
-
-
-
gamma-aminobutyrate transaminase
-
-
-
-
gamma-aminobutyric acid aminotransferase
-
-
-
-
gamma-aminobutyric acid transaminase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
mechanism
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
mechanism
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
mechanism
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
mechanism
Candida guilliermondii var. membranaefaciens
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
gamma-aminobutyric acid transaminase and beta-alanine transaminase are identical
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
active site comparison with pig enzyme and with dialkylglycine decarboxylase
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
mechanism
Candida guilliermondii var. membranaefaciens Y43
-
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
4-aminobutanoate:2-oxoglutarate aminotransferase
Requires pyridoxal phosphate. Some preparations also act on beta-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate.
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CAS REGISTRY NUMBER
COMMENTARY
9037-67-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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,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-aminopropanesulfonate + 2-oxoglutarate
3-sulfopropanal + L-glutamate
substrate is homotaurine
-
-
?
4-aminobutyrate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
DL-3-amino-1-cyclopentene-1-carboxylic acid + 2-oxoglutarate
3-oxo-1-cyclopentene-1-carboxylic acid + L-glutamate
-
analogue of 4-aminobutanoate, vigabatrin
-
-
?
hypotaurine + 2-oxoglutarate
L-glutamate + 2-oxoethanesulfinic acid
-
poor amino donor
-
-
r
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
-
?
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanol
-
poor amino donor
-
-
r
[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
-
-
?
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
-
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
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
-
-
-
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
-
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
-
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
-
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
-
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
-
-
-
?
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
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
Q9AGD3
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
Q9AGD3
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
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
involved in beta-alanine metabolism
-
-
-
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
-
-
-
?
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
-
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
-
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
-
transamination at 29% the rate of 4-aminobutanoate
-
-
-
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
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
-
-
?
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
-
-
-
-
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
-
effective amino group donor
-
-
r
D-lysine + 2-oxoglutarate
L-glutamate + 5-aminopentanol
-
poor amino donor
-
-
r
D-lysine + 2-oxoglutarate
L-glutamate + 5-aminopentanol
-
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
-
-
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
no amino acceptors are oxaloacetate, pyruvate
-
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-aminopropanesulfonate + 2-oxoglutarate
3-sulfopropanal + L-glutamate
Q0K2K2
substrate is homotaurine
-
-
?
4-aminobutyrate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
Q0K2K2
-
-
-
?
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
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
Q9AGD3
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
no activation by addition of pyridoxal phosphate, but sensitive to carbonyl reagents
pyridoxal 5'-phosphate
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+/-)-(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
(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,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)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid
-
mechanism-based inactivator, reacts via aromatization mechanism
2,4-dimethylphenyl semicarbazide hydrochloride
-
90% inhibition at 0.0625 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
4-amino-2-fluorobutanoate
-
reversible, competitive to 4-aminobutanoate
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
6-Azauracil
-
63% inhibition at 1 mM, reversible by dialysis, not by pyridoxal phosphate addition
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
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+
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
falcarindiol
-
active-site directed, irreversible, 23% residual activity at 14 mM, isolate of root of Angelica dahurica
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
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-(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
Ni2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
propan-2-one N-(2,4-dimethylphenyl)semicarbazone
-
44% inhibition at 0.25 mM
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+
4-aminohex-5-enoic acid
-
i.e. gamma-vinyl GABA, competitive, does not affect transamination process of 2-oxoglutarate
beta-Alanine
competitive inhibitor of pyruvate-dependent GABA-T activity
Cu2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
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
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
ornithine
competitive inhibitor of pyruvate-dependent GABA-T activity
vigabatrin
competitive inhibitor of pyruvate-dependent GABA-T activity
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
-
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
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
-
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
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-aminobutyrate
induction during growth with 4-aminobutyrate (GABA)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
4-Oxobutanoate
with L-alanine as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
2.4
L-alanine
with 4-oxobutanoate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
8
tetrazole-5-butanamine
-
at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
2.3
tetrazole-5-ethanamine
-
at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
2.4
tetrazole-5-propanamine
-
at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
0.22
2-oxoglutarate
in 100 mM potassium phosphate (pH 8.0), 0.1 mM pyridoxal 5'-phosphate; pH 8.0, 30°C
0.18
4-aminobutanoate
with glyoxylate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
0.34
4-aminobutanoate
with pyruvate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
2.4
4-aminobutanoate
-
at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol; pH 8.5
3.2
4-aminobutanoate
in 100 mM potassium phosphate (pH 8.0), 0.1 mM pyridoxal 5'-phosphate
0.0165
glyoxylate
pH 9, 25°C, fixed substrate: 4-aminobutanoate
0.11
glyoxylate
in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
0.14
pyruvate
in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
additional information
additional information
-
kinetic study; pH-dependence of kinetic data
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.8
4-Oxobutanoate
with L-alanine as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
15.4
L-alanine
with 4-oxobutanoate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
0.693
tetrazole-5-butanamine
-
at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
0.265
tetrazole-5-ethanamine
-
at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
0.477
tetrazole-5-propanamine
-
at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
0.817
4-aminobutanoate
-
at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
6.9
4-aminobutanoate
with glyoxylate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
10.6
4-aminobutanoate
with pyruvate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
9.7
glyoxylate
in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
10.6
pyruvate
in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
770
4-Oxobutanoate
with L-alanine as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
6.4
L-alanine
with 4-oxobutanoate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
31
4-aminobutanoate
with pyruvate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
39
4-aminobutanoate
with glyoxylate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
88
glyoxylate
in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
76
pyruvate
in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
(1R,4S)-4-amino-3-fluorocyclopent-2-enecarboxylic acid
-
in potassium diphosphate buffer (pH 8.5)
2.8
(1R,4S)-4-amino-3-pentafluoroethylcyclopent-2-enecarboxylic acid
-
in potassium diphosphate buffer (pH 8.5)
4.2
(1S,3S)-3-amino-4-(2,2,2-trifluoro-1-trifluoromethylethylidene)-cyclopentanecarboxylic acid
-
in potassium diphosphate buffer (pH 8.5)
3.75
(1S,4S)-2-(difluoromethylidene)-4-(1H-tetrazol-5-yl)cyclopentanamine
-
pH 6.5
0.598
2-N-(acetylamino)cyclohexane sulfonic acid
-
competitive inhibition at 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
1-(4-acetylphenyl)-3-(4-bromophenyloxy)-pyrrolidine-2,5-dione
Mus musculus
-
pH 7.5, 37°C
0.16
1-(4-acetylphenyl)-3-(salicyldehydoxy)-pyrrolidine-2,5-dione
Mus musculus
-
pH 7.5, 37°C
0.086
N-(4-bromophenyl)-3-(4-chlorophenyl)-6,7-dimethoxy-3a,4-dihydroindeno[1,2-c]pyrazole-2(3H)-carboxamide
Sus scrofa
-
predicted value, pH not specified in the publication, temperature not specified in the publication
0.149
N-(4-bromophenyl)-3-(4-fluorophenyl)-6,7-dimethoxy-3a,4-dihydroindeno[1,2-c]pyrazole-2(3H)-carboxamide
Sus scrofa
-
predicted value, pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0183
isoform GABA-T2, using pyruvate as amino cceptor
0.0209
isoform GABA-T2, using glyoxylate as amino cceptor
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
1.6
substrate gamma-aminobutanoate, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30°C
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
4.9
5.79
isoform GABA-T1, using pyruvate as amino acceptor
12.8
substrate gamma-aminobutanoate, continuous assay with succinate dehydrogenase, pH 8.0, 30°C; using 4-aminobutanoate as substrate
additional information
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; 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; 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; 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; specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 226% with 5-aminovalerate 6-aminocapronate as substrate; specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 25% with 6-aminocapronate as substrate; specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 270% with 4-aminobutyrate as substrate; 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; 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; 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; 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; 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; 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; 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; specific activity with 3-aminopropanoate, taurine, (S)-cysteate, 3-aminopropanol or 4-aminobutanol as substrates is not detected
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; 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; 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; 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; specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 226% with 5-aminovalerate 6-aminocapronate as substrate; specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 25% with 6-aminocapronate as substrate; specific activity, normalized to that with homotaurine (100%: 271 mkat/kg protein), is 270% with 4-aminobutyrate as substrate; 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; 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; 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; 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; 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; 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; 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; specific activity with 3-aminopropanoate, taurine, (S)-cysteate, 3-aminopropanol or 4-aminobutanol as substrates is not detected
additional information
-
3.4 units/mg in crude brain homogenate and 51.2 units/mg after 15fold purification
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
8.7
additional information
additional information
-
pI: 5.9 and 6.35 (isozyme II), pI: 6.1 and 6.3 (isozyme I)
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4 - 9
-
about half-maximal activity at pH 7.4 and about 90% of maximal activity at pH 9
8 - 9.2
8 - 9.2
-
about 60% of maximal activity at pH 9.2; about half-maximal activity at pH 8
8 - 9.2
-
about 50% of maximal activity at pH 9.2; about half-maximal activity at pH 8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
45
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
Candida guilliermondii var. membranaefaciens
-
linear increase, above 45°C rapid decrease
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
isoform Pyd4, involved in both beta-alanine and gamma-aminobutanoic acid transamination
UniProt
brenda
-
636963, 637038, 637040, 637041, 637045, 637049, 637050, 637052, 637062, 637065, 637067, 637072, 637080, 672598, 673052, 675524, 687360, 705278, 706140
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
highest expression in ripe fruit leaf at day 92; highest expression of in ripe fruit leaf at day 92; highest expression of in ripe fruit leaf at day 92
brenda
transcripts of gamma-aminobutanoate transaminase and glutamic acid decarboxylase 65, and glutamic acid decarboxylase 67 are detected throughout the brain, largely in the ventral and medial regions of telencephalon, nucleus preopticus, nucleus recessus lateralis of the hypothalamus, and Purkinje cell layer of the cerebellum
brenda
transcripts of gamma-aminobutanoate transaminase and glutamic acid decarboxylase 65, and glutamic acid decarboxylase 67 are detected throughout the brain, largely in the ventral and medial regions of telencephalon, nucleus preopticus, nucleus recessus lateralis of the hypothalamus, and Purkinje cell layer of the cerebellum
brenda
transcripts of gamma-aminobutanoate transaminase and glutamic acid decarboxylase 65, and glutamic acid decarboxylase 67 are detected throughout the brain, largely in the ventral and medial regions of telencephalon, nucleus preopticus, nucleus recessus lateralis of the hypothalamus, and Purkinje cell layer of the cerebellum
brenda
enzyme activity of gamma-aminobutanoate transaminase is highest in the hypothalamus and optic tectum
brenda
; transcripts of gamma-aminobutanoate transaminase and glutamic acid decarboxylase 65, and glutamic acid decarboxylase 67 are detected throughout the brain, largely in the ventral and medial regions of telencephalon, nucleus preopticus, nucleus recessus lateralis of the hypothalamus, and Purkinje cell layer of the cerebellum. Enzyme activity of gamma-aminobutanoate transaminase is highest in the hypothalamus and optic textum. Gamma-aminobutanoate transaminase activity is significantly higher than total glutamic acid decarboxylase activity
brenda
-
-
brenda
-
-
637033, 637036, 637038, 637048, 637058, 637073, 637075, 637076, 637081, 661332, 672536, 675313, 685115, 721841, 721847, 738454
brenda
; enzyme activity of gamma-aminobutanoate transaminase is highest in the hypothalamus and optic textum
brenda
induction during leaf senescence with highest level at the S3 senescent stage
brenda
transcripts of gamma-aminobutanoate transaminase and glutamic acid decarboxylase 65, and glutamic acid decarboxylase 67 are detected throughout the brain, largely in the ventral and medial regions of telencephalon, nucleus preopticus, nucleus recessus lateralis of the hypothalamus, and Purkinje cell layer of the cerebellum
brenda
-
biochemical and histochemical data to distribution, young to elderly men
brenda
-
mostly arteries and partly veins of, strong decrease of activity with age
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
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
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
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
-
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
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
Show AA Sequence and Transmembrane Helices (6027 entries)
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