Information on EC 2.6.1.19 - 4-aminobutyrate-2-oxoglutarate transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.6.1.19
-
RECOMMENDED NAME
GeneOntology No.
4-aminobutyrate-2-oxoglutarate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
show the reaction diagram
mechanism
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
show the reaction diagram
mechanism
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
show the reaction diagram
mechanism
Candida guilliermondii var. membranaefaciens
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
show the reaction diagram
gamma-aminobutyric acid transaminase and beta-alanine transaminase are identical
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
show the reaction diagram
active site comparison with pig enzyme and with dialkylglycine decarboxylase
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
show the reaction diagram
mechanism
Candida guilliermondii var. membranaefaciens Y43
-
-
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-aminobutyrate degradation
-
4-aminobutyrate degradation II
-
4-aminobutyrate degradation III
-
4-aminobutyrate degradation V
-
Alanine, aspartate and glutamate metabolism
-
beta-alanine degradation I
-
beta-Alanine metabolism
-
Butanoate metabolism
-
GABA shunt
-
glutamate degradation IV
-
Metabolic pathways
-
nicotine degradation I
-
Propanoate metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4-aminobutyrate aminotransferase
-
-
-
-
4-aminobutyrate aminotransferase
-
-
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
-
-
-
-
aminobutyrate transaminase
Q0K2K2
-
aminotransferase, aminobutyrate
-
-
-
-
beta-alanine aminotransferase
-
-
-
-
beta-alanine transaminase
-
-
-
-
beta-alanine-oxoglutarate aminotransferase
-
-
-
-
beta-alanine-oxoglutarate transaminase
-
-
-
-
GABA aminotransferase
-
-
-
-
GABA aminotransferase
-
-
GABA aminotransferase
-
-
GABA transaminase
-
-
-
-
GABA transaminase
-
-
GABA transaminase
-
-
GABA transaminase
Q2PZI2
-
GABA transaminase
Q0K2K2
-
GABA transaminase
-
-
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
Q94FS9
-
GABA-T
Q2PZI2
-
GABA-T
J9XGP8, J9XGZ5
-
GABA-T
-
-
GABA-T
-
-
GABA-T
-
-
GABA-T1
Q84P54
isoform
GABA-T2
Q84P53
isoform
GABA-T3
Q84P52
isoform
GABA-transaminase
-
-
GABA:2-oxoglutarate aminotransferase
Q0K2K2
-
GabT
Q0K2K2
-
gamma-aminobutyrate aminotransaminase
-
-
-
-
gamma-aminobutyrate aminotransferase
-
-
gamma-aminobutyrate transaminase
-
-
-
-
gamma-aminobutyrate transaminase
-
-
gamma-aminobutyrate transaminase
Q94FS9
-
gamma-aminobutyrate transaminase
J9XGP8, J9XGZ5
-
gamma-aminobutyrate transaminase
-
-
gamma-aminobutyrate transaminase
-
-
gamma-aminobutyrate transaminases
Q84P52, Q84P53, Q84P54
-
gamma-aminobutyrate-alpha-ketoglutarate aminotransferase
-
-
-
-
gamma-aminobutyrate-alpha-ketoglutarate transaminase
-
-
-
-
gamma-aminobutyrate: GABA transaminase
-
-
gamma-aminobutyrate:alpha-oxoglutarate aminotransferase
-
-
-
-
gamma-aminobutyric acid aminotransferase
-
-
-
-
gamma-aminobutyric acid aminotransferase
-
-
gamma-aminobutyric acid pyruvate transaminase
-
-
-
-
gamma-aminobutyric acid transaminase
-
-
-
-
gamma-aminobutyric acid transaminase
Q84P52, Q84P53, Q84P54
-
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
-
-
-
-
homotaurine:2-oxoglutarate aminotransferase
Q0K2K2
-
MdGABA-T1
J9XGP8
-
MdGABA-T2
J9XGZ5
-
Osl2
Q71SH3
-
pollen-pistil incompatibility 2
-
-
CAS REGISTRY NUMBER
COMMENTARY
9037-67-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
subunit
Q94FS9
UniProt
Manually annotated by BRENDA team
Candida guilliermondii var. membranaefaciens
Y43
-
-
Manually annotated by BRENDA team
Candida guilliermondii var. membranaefaciens Y43
Y43
-
-
Manually annotated by BRENDA team
fragment
TrEMBL
Manually annotated by BRENDA team
streptomycin-bleached mutant strain
-
-
Manually annotated by BRENDA team
Euglena gracilis mutant
streptomycin-bleached mutant strain
-
-
Manually annotated by BRENDA team
isoform Pyd4, involved in both beta-alanine and gamma-aminobutanoic acid transamination
UniProt
Manually annotated by BRENDA team
isoform Uga1
UniProt
Manually annotated by BRENDA team
Mongolian gerbil
-
-
Manually annotated by BRENDA team
Swiss albino
-
-
Manually annotated by BRENDA team
two isozymes, mitochondrial GABA-T and synaptosomal GABA-T
-
-
Manually annotated by BRENDA team
wild-type strain 3a6A
-
-
Manually annotated by BRENDA team
-
Q71SH3
Swissprot
Manually annotated by BRENDA team
Pseudomonas sp. F-126
F-126
-
-
Manually annotated by BRENDA team
weanling
-
-
Manually annotated by BRENDA team
isoform Uga1
UniProt
Manually annotated by BRENDA team
isoform Uga1
UniProt
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
metabolism
-, Q0K2K2
GABA metabolism
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
Q84P52, Q84P53, Q84P54, -
isoform GABA-T1 plays the predominant role in GABA metabolism in vegetative tissue
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1R,4S)-4-amino-2-cyclopentene-1-carboxylic acid + 2-oxoglutarate
? + L-glutamate
show the reaction diagram
-
analogue of 4-aminobutanoate, vigabatrin
-
-
?
(4R)-4-amino-1-cyclopentene-1-carboxylic acid + 2-oxoglutarate
4-oxo-1-cyclopentene1-carboxylic acid + L-glutamate
show the reaction diagram
-
analogue of 4-aminobutanoate, vigabatrin
-
-
?
(R)-4-amino-3-fluorobutanoic acid
4-aminobut-2-enoic acid + HF
show the reaction diagram
-
-
-
-
?
(R,S)-4-amino-3-fluorobutanoic acid
4-aminobut-2-enoic acid + HF
show the reaction diagram
-
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
show the reaction diagram
-
mechanism-based inactivator that partly undergoes inactivation
-
-
?
1H-tetrazole-5-butanamine + 2-oxoglutarate
(1H-tetrazol-5-yl)-butyraldehyde + L-glutamate
show the reaction diagram
-
-
-
-
?
1H-tetrazole-5-ethanamine + 2-oxoglutarate
(1H-tetrazol-5-yl)-acetaldehyd + L-glutamate
show the reaction diagram
-
-
-
-
?
1H-tetrazole-5-propanamine + 2-oxoglutarate
(1H-tetrazol-5-yl)-propionaldehyde + L-glutamate
show the reaction diagram
-
-
-
-
?
3-(aminomethyl)benzoic acid + 2-oxoglutarate
3-(iminomethyl)benzoic acid + L-glutamate
show the reaction diagram
-
3.4% of the activity with 4-aminobutanoate
-
-
?
3-aminoisobutanoate + 2-oxoglutarate
L-glutamate + 3-oxoisobutanoate
show the reaction diagram
-
-
-
-
r
3-aminoisobutanoate + 2-oxoglutarate
L-glutamate + 3-oxoisobutanoate
show the reaction diagram
-
transamination at 14% the rate of 4-aminobutanoate
-
-
r
3-aminoisobutanoate + 2-oxoglutarate
L-glutamate + 3-oxoisobutanoate
show the reaction diagram
-
transamination at 55% the rate of 4-aminobutanoate
-
-
r
3-aminopropanesulfonate + 2-oxoglutarate
3-sulfopropanal + L-glutamate
show the reaction diagram
-, Q0K2K2
substrate is homotaurine
-
-
?
4-(aminomethyl)-1H-pyrrole-2-carboxylic acid + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
4-(aminomethyl)furan-2-carboxylic acid + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
4-(aminomethyl)furan-3-carboxylic acid + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
4-(aminomethyl)thiophene-2-carboxylic acid + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
4-(aminomethyl)thiophene-3-carboxylic acid + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
P50554
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Q9AGD3
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
A5H0J5, A5H0J6, -
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Q71SH3
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-, Q2PZI2
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
P17649
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
O13837, -
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
A5H0J5, A5H0J6, -
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
best substrate
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Candida guilliermondii var. membranaefaciens
-
best substrate
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
specific for 2-oxoglutarate
i.e. succinic semialdehyde + L-Glu
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
no substrate: 2-oxoglutarate
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
inducible enzyme
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
involved in gamma-aminobutyrate metabolism
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
involved in beta-alanine metabolism
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Q9AGD3
involved in 4-aminobutanoate metabolism via the GABA shunt pathway
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
best substrate at pH 9.5 as well as at pH 8.5
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Euglena gracilis mutant
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Euglena gracilis mutant
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Pseudomonas sp. F-126
-
-
-
r
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Pseudomonas sp. F-126
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Nicotiana tabacum Samsun N.N.
-
no substrate: 2-oxoglutarate
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Candida guilliermondii var. membranaefaciens Y43
-
best substrate
-
r
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
show the reaction diagram
Q84P52, Q84P53, Q84P54, -
-
-
-
?
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
show the reaction diagram
Q94FS9
-
-
-
?
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
show the reaction diagram
J9XGP8, J9XGZ5
-
-
-
?
4-aminobutanoate + glyoxylate
4-oxobutanoate + glycine
show the reaction diagram
Pseudomonas sp., Pseudomonas sp. F-126
-
at 16% of the activity of 2-oxoglutarate
-
-
r
4-aminobutanoate + pyruvate
4-oxobutanoate + alanine
show the reaction diagram
-
not using 2-oxoglutarate
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + alanine
show the reaction diagram
-
at 7% of the activity of 2-oxoglutarate
-
-
r
4-aminobutanoate + pyruvate
4-oxobutanoate + alanine
show the reaction diagram
Nicotiana tabacum Samsun N.N.
-
not using 2-oxoglutarate
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
show the reaction diagram
Q84P52, Q84P53, Q84P54, -
-
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
show the reaction diagram
Q94FS9
-
-
-
?
4-aminobutanoate + pyruvate
4-oxobutanoate + L-alanine
show the reaction diagram
J9XGP8, J9XGZ5
-
-
-
?
4-aminobutyrate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-, Q0K2K2
-
-
-
?
5-(aminomethyl)-1H-pyrrole-2-carboxylic acid + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
5-(aminomethyl)furan-2-carboxylic acid + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
5-(aminomethyl)thiophene-2-carboxylic acid + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
show the reaction diagram
-
-
-
-
-
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
show the reaction diagram
-
-
-
-
-
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
show the reaction diagram
-
not
-
-
-
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
show the reaction diagram
-
transamination at 48% the rate of 4-aminobutanoate
-
-
-
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
show the reaction diagram
-
transamination at 60% the rate of 4-aminobutanoate
-
-
-
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
show the reaction diagram
Candida guilliermondii var. membranaefaciens
-
transamination at 45% the rate of 4-aminobutanoate
-
-
-
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
show the reaction diagram
-
transamination at 85% the rate of 4-aminobutanoate
-
-
-
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
show the reaction diagram
Candida guilliermondii var. membranaefaciens Y43
-
transamination at 45% the rate of 4-aminobutanoate
-
-
-
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
show the reaction diagram
-
-
-
-
-
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
show the reaction diagram
-
not
-
-
-
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
show the reaction diagram
Candida guilliermondii var. membranaefaciens
-
transamination at 27% the rate of 4-aminobutanoate
-
-
-
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
show the reaction diagram
-
transamination at 29% the rate of 4-aminobutanoate
-
-
-
6-aminohexanoate + 2-oxoglutarate
L-glutamate + 6-oxohexanoate
show the reaction diagram
Candida guilliermondii var. membranaefaciens Y43
-
transamination at 27% the rate of 4-aminobutanoate
-
-
-
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
-
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
-
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
P17649
-
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
O13837, -
-
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
A5H0J5, A5H0J6, -
-
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
not
-
-
-
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
not
-
-
-
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
not
-
-
-
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
Candida guilliermondii var. membranaefaciens
-
poor substrate
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
effective amino group donor
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
-
effective amino group donor
-
-
r
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
Pseudomonas sp. F-126
-
not
-
-
-
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
show the reaction diagram
Candida guilliermondii var. membranaefaciens Y43
-
poor substrate
-
-
r
cadaverine + 2-oxoglutarate
L-glutamate + ?
show the reaction diagram
-
poor amino donor
-
-
r
cadaverine + 2-oxoglutarate
L-glutamate + 5-aminopentanal
show the reaction diagram
-
-
-
-
?
D-lysine + 2-oxoglutarate
L-glutamate + 5-aminopentanol
show the reaction diagram
-
poor amino donor
-
-
r
D-lysine + 2-oxoglutarate
L-glutamate + 5-aminopentanol
show the reaction diagram
-
poor amino donor
-
-
r
DL-3-amino-1-cyclopentene-1-carboxylic acid + 2-oxoglutarate
3-oxo-1-cyclopentene-1-carboxylic acid + L-glutamate
show the reaction diagram
-
analogue of 4-aminobutanoate, vigabatrin
-
-
?
DL-3-hydroxy-4-aminobutanoate + 2-oxoglutarate
L-glutamate + 3-hydroxy-4-oxobutanoate
show the reaction diagram
-
-
-
-
r
DL-3-hydroxy-4-aminobutanoate + 2-oxoglutarate
L-glutamate + 3-hydroxy-4-oxobutanoate
show the reaction diagram
-
-
-
-
r
DL-3-hydroxy-4-aminobutanoate + 2-oxoglutarate
L-glutamate + 3-hydroxy-4-oxobutanoate
show the reaction diagram
-
transamination at 20% the rate of 4-aminobutanoate
-
-
r
DL-ornithine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
show the reaction diagram
-
not
-
-
-
DL-ornithine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
show the reaction diagram
-
poor amino donor
-
-
-
DL-ornithine + 2-oxoglutarate
L-glutamate + 4-methyl-2-oxopentanoate
show the reaction diagram
-
poor amino donor
-
-
-
gamma-aminobutyric acid
?
show the reaction diagram
-
-
-
-
?
hypotaurine + 2-oxoglutarate
L-glutamate + 2-oxoethanesulfinic acid
show the reaction diagram
-
not
-
-
-
hypotaurine + 2-oxoglutarate
L-glutamate + 2-oxoethanesulfinic acid
show the reaction diagram
-
poor amino donor
-
-
r
L-lysine + 2-oxoglutarate
L-glutamate + (S)-2-amino-6-oxohexanoate
show the reaction diagram
-
-
i.e. L-2-aminoadipate-6-semialdehyde
-
?
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanol
show the reaction diagram
-
poor amino donor
-
-
r
putrescine + 2-oxoglutarate
L-glutamate + 4-aminobutanal
show the reaction diagram
-
-
-
-
?
tetrazole-5-butanamine + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
tetrazole-5-ethanamine + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
tetrazole-5-propanamine + 2-oxoglutarate
?
show the reaction diagram
-
-
-
-
?
[2-(aminomethyl)phenyl]acetic acid + 2-oxoglutarate
(2-formylphenyl)acetic acid + L-glutamate
show the reaction diagram
-
5.65% of the activity with 4-aminobutanoate
-
-
?
[3-(aminomethyl)phenyl]acetic acid + 2-oxoglutarate
(3-formylphenyl)acetic acid + L-glutamate
show the reaction diagram
-
0.78% of the activity with 4-aminobutanoate
-
-
?
L-ornithine + 2-oxoglutarate
L-glutamate + (S)-2-amino-5-oxopentanoate
show the reaction diagram
-
-
i.e. L-glutamate-gamma-semialdehyde
-
?
additional information
?
-
-
overview
-
-
-
additional information
?
-
-
overview
-
-
-
additional information
?
-
-
overview
-
-
-
additional information
?
-
-
no amino acceptors are oxaloacetate, pyruvate
-
-
-
additional information
?
-
-
no amino acceptors are oxaloacetate, pyruvate
-
-
-
additional information
?
-
-
no amino acceptors are oxaloacetate, pyruvate
-
-
-
additional information
?
-
-
no substrates are taurine, 3-aminopropane sulfonate, glycine
-
-
-
additional information
?
-
-
no substrate: lysine
-
-
-
additional information
?
-
Candida guilliermondii var. membranaefaciens
-
no substrates are L-aminovalerate, L-norleucine, straight alpha-amino acids, diamino acids
-
-
-
additional information
?
-
-
no amino acceptors are 2-oxobutyrate, phenylpyruvate, alpha-ketoadipate
-
-
-
additional information
?
-
-
no amino acceptors are ketomalonic acid, alpha-ketoisovaleric acid, aspartate, L-2,4-diaminoglutarate, alanine, D-glutamate or malonic semialdehyde cannot replace L-glutamate or succinic semialdehyde in the reverse reaction
-
-
-
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
?
-
A5H0J5, A5H0J6, -
does not use pyruvate as amino acceptor
-
-
-
additional information
?
-
Q94FS9
cannot utilize 2-oxoglutarate as amino acceptor
-
-
-
additional information
?
-
Pseudomonas sp. F-126
-
no substrates are taurine, 3-aminopropane sulfonate, glycine
-
-
-
additional information
?
-
Candida guilliermondii var. membranaefaciens Y43
-
no substrates are L-aminovalerate, L-norleucine, straight alpha-amino acids, diamino acids
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-aminopropanesulfonate + 2-oxoglutarate
3-sulfopropanal + L-glutamate
show the reaction diagram
-, Q0K2K2
substrate is homotaurine
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
inducible enzyme
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
involved in gamma-aminobutyrate metabolism
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-
involved in beta-alanine metabolism
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Q9AGD3
involved in 4-aminobutanoate metabolism via the GABA shunt pathway
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Euglena gracilis mutant
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
Pseudomonas sp. F-126
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
-
4-aminobutyrate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
show the reaction diagram
-, 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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
no activation by addition of pyridoxal phosphate, but sensitive to carbonyl reagents
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
2 mol per mol enzyme
pyridoxal 5'-phosphate
-
requirement, bound to lysine-residue 330
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
K357 is involved in binding
pyridoxal 5'-phosphate
-
0.1 mM
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-, Q2PZI2
0.01 mM
pyridoxal 5'-phosphate
A5H0J5, A5H0J6, -
;
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-, Q0K2K2
cofactor remains bound during purification
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q84P52, Q84P53, Q84P54, -
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
J9XGP8, J9XGZ5
;
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Iron
-
iron-sulfur cluster
Iron
-
2Fe-2S-cluster
additional information
-
no iron-sulfur cluster
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
(+/-)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,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
(Z)-4-amino-2-butenoic acid
-
-
1H-tetrazole-5-(alpha-vinyl-propanamine)
-
-
2,4-diaminobutanoate
-
kinetics
2,4-diaminobutanoate
-
not
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
-
-
2-oxoadipic acid
-
-
2-oxoglutarate
-
-
2-oxoglutarate
-
-
2-oxoglutarate
Candida guilliermondii var. membranaefaciens
-
-
2-oxoglutarate
-
substrate inhibiton
2-Thiouracil
-
weak
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-(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-enoic acid
-
-
4-aminohex-5-enoic acid
-
i.e. gamma-vinyl GABA, competitive, does not affect transamination process of 2-oxoglutarate
4-Aminohex-5-ynoic acid
-
irreversible, in vitro and in vivo, kinetics
4-ethynyl-4-aminobutanoate
-
-
4-hydroxybenzaldehyde
-
potent inhibitor
4-hydroxybenzaldehyde
-
IC50: 0.0165 mM, competitive inhibition
4-hydroxybenzaldehyde
-
competitive inhibitor of GABA transaminase
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
J9XGP8, J9XGZ5
;
-
5-Diazouracil
-
weak
5-Fluorouracil
-
weak
5-Fluorouracil
-
-
5-Iodouracil
-
84% inhibition at 1 mM
5-Nitrouracil
-
weak
5-Thiouracil
-
weak
6-Azathymine
-
-
6-Azauracil
-
63% inhibition at 1 mM, reversible by dialysis, not by pyridoxal phosphate addition
acetic acid
-
-
Adipic acid
-
-
ADP
-
reversible
alpha-alanine
Candida guilliermondii var. membranaefaciens
-
-
Aminooxyacetate
-
-
Aminooxyacetate
-
kinetics
Aminooxyacetate
-
99% inhibition at 1 mM
Aminooxyacetate
-
-
Aminooxyacetate
-
-
Aminooxyacetate
-
80% inhibition at 2 mM
Aminooxyacetate
P22256
-
Aminooxyacetate
J9XGP8, J9XGZ5
;
ATP
-
reversible
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-Alanine
Candida guilliermondii var. membranaefaciens
-
-
beta-Alanine
Q94FS9
competitive inhibitor of pyruvate-dependent GABA-T activity
beta-Alanine
J9XGP8, J9XGZ5
moderate inhibitor; moderate inhibitor
Branched-chain fatty acids
-
-
-
Butyric acid
-
-
Butyric acid
Candida guilliermondii var. membranaefaciens
-
-
Ca2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
Carbonyl reagents
-
-
-
Carbonyl reagents
-
-
-
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+
Cu2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
Cycloserine
-
90% inhibition at 1 mM
D-cycloserine
-
-
D-penicillamine
-
-
D-penicillamine
-
-
Dioxan
-
5% v/v
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-cysteine
-
-
DL-trans-4-amino-2-cyclopentene-1-carboxylic acid
-
analogue of 4-aminobutanoate, vigabatrin
ethanol
-
10% v/v, weak
ethanol
-
in presence of disulfiram, i.e. N,N,N,N-tetraethylthiuram disulfide
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
gabaculine
-
98% inhibition at 1 mM
gabaculine
-
i.e. 5-amino-1,3-cyclohexadienylcarboxylate, ir, kinetics; not its tert-butylcarbamate derivative
gabaculine
-
80% inhibition at 2 mM
gabaculine
-
IC50: 0.0018 mM, potent and irreversible inhibitor
gabaculine
-
highly specific GABAtransaminase inhibitor
gamma-vinyl 4-aminobutanoate
-
0.1 mM, complete inhibition
gastrodigenin
-
30.87% inhibition at 0.01 mM
GDP
-
reversible
glutamic acid
-
-
glycine
Q94FS9
competitive inhibitor of pyruvate-dependent GABA-T activity
HgCl2
-
strong, 50% inhibition at 0.007 mM
HgCl2
-
24% inhibition at 0.05 mM, pyridoxal 5'-phosphate protects
hydrazine
-
-
hydroxylamine
-
-
hydroxylamine
-
-
imperatorin
-
active-site directed, irreversible, 14% residual activity at 14 mM, isolate of root of Angelica dahurica
Lysyl reagents
-
2-oxoglutarate protects
-
Maleate
-
-
-
methanol
-
10% v/v, weak
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+
monoiodoacetate
-
not
Muscimol
-
i.e. 5-(aminomethyl)-3-isoxazolol
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
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
ornithine
Q94FS9
competitive inhibitor of pyruvate-dependent GABA-T activity
ornithine
J9XGP8, J9XGZ5
moderate inhibitor; moderate inhibitor
p-chloromercuribenzoate
-
strong
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
phenylhydrazine
-
-
phenylhydrazine
-
-
pimelic acid
-
-
propan-2-one N-(2,4-dimethylphenyl)semicarbazone
-
44% inhibition at 0.25 mM
Propionic acid
-
-
Propionic acid
Candida guilliermondii var. membranaefaciens
-
-
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
SH-group reagents
-
2-oxoglutarate protects
-
SH-group reagents
-
-
-
SH-group reagents
-
2-mercaptoethanol or DTT reactivates
-
SH-group reagents
-
-
-
Sr2+
-
order of decreasing inhibitory potency: Hg2+, Cd2+, Cu2+, Co2+, Ba2+, Sr2+, Ni2+, Mn2+, Ca2+, Mg2+
Succinic semialdehyde
-
substrate inhibition
Succinic semialdehyde
-
-
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
vigabatrin
-
gamma-vinyl GABA, anticonvulsant, induces spontaneous release of 4-aminobutanoate
vigabatrin
-
mechanism
vigabatrin
-
IC50: 0.35 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
-
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
Q94FS9
competitive inhibitor of pyruvate-dependent GABA-T activity
vigabatrin
-
complete inhibition at 0.5 mM
[2-(aminomethyl)phenyl]acetic acid
-
poor competitive inhibitor
[3-(aminomethyl)phenyl]acetic acid
-
poor competitive inhibitor
monoiodoacetate
-
-
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 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
-
no inhibition by chelating agents, non-substrate L- or D-amino acids, metal ions
-
additional information
-
no substrate inhibition: 4-aminobutanoate
-
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
-
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)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4-aminobutyrate
-, Q0K2K2
induction during growth with 4-aminobutyrate (GABA)
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
(4R)-4-amino-1-cyclopentene-1-carboxylic acid
-
-
1.6
-
(4R)-4-amino-1-cyclopentene-1-carboxylic acid
-
-
0.059
-
(R)-4-amino-3-fluorobutanoic acid
-
pH 8.5
0.045
-
(R,S)-4-amino-3-fluorobutanoic acid
-
pH 8.5
8
-
1H-tetrazole-5-butanamine
-
pH 8.5
2.3
-
1H-tetrazole-5-ethanamine
-
pH 8.5
2.4
-
1H-tetrazole-5-propanamine
-
pH 8.5
0.0021
-
2-oxoglutarate
-
mutant E211S, 25C, pH 7.8
0.063
-
2-oxoglutarate
-
mutant E211S/I50H/V80T, 25C, pH 7.8
0.11
-
2-oxoglutarate
-
25C, pH 8.4
0.13
0.27
2-oxoglutarate
-
37C, pH 8.0
0.13
0.27
2-oxoglutarate
-
37C, pH 7.3
0.13
0.27
2-oxoglutarate
-
-
0.13
-
2-oxoglutarate
-
mutant V241A, 25C, pH 7.8
0.22
-
2-oxoglutarate
-
pH 8.5
0.22
-
2-oxoglutarate
A5H0J5, A5H0J6, -
in 100 mM potassium phosphate (pH 8.0), 0.1 mM pyridoxal 5'-phosphate; pH 8.0, 30C
0.27
-
2-oxoglutarate
-
pH 8.5
0.47
-
2-oxoglutarate
-
pH 8.6, 25C
0.7
-
2-oxoglutarate
-
37C
0.72
-
2-oxoglutarate
-
mutant E211S/I50G/C77K, 25C, pH 7.8
0.75
-
2-oxoglutarate
-
-
0.78
-
2-oxoglutarate
-
mutant I50Q/G295Y, 25C, pH 7.8
1
-
2-oxoglutarate
-
-
1
-
2-oxoglutarate
-
pH 8.4, 25C
1.07
-
2-oxoglutarate
-
wild-type, 25C, pH 7.8
1.3
1.5
2-oxoglutarate
-
-
1.5
-
2-oxoglutarate
Candida guilliermondii var. membranaefaciens
-
-
2.1
-
2-oxoglutarate
A5H0J5, A5H0J6, -
pH 8.0, 30C
2.8
-
2-oxoglutarate
-
pH 8.0, 37C
5.5
-
2-oxoglutarate
-
38C, pH 8.5
6.3
-
2-oxoglutarate
-, Q0K2K2
Km apparent value
8.3
-
2-oxoglutarate
-
pH 8.0, 37C
46
-
2-oxoglutarate
-
mutant I50Q, 25C, pH 7.8
8.5
-
3-Aminopropanesulfonate
-, Q0K2K2
Km apparent value
1.4
-
4-(aminomethyl)-1H-pyrrole-2-carboxylic acid
-
pH 8.5, 25C
-
0.31
-
4-(aminomethyl)furan-2-carboxylic acid
-
pH 8.5, 25C
-
2.8
-
4-(aminomethyl)furan-3-carboxylic acid
-
pH 8.5, 25C
-
1.7
-
4-(aminomethyl)thiophene-2-carboxylic acid
-
pH 8.5, 25C
-
10
-
4-(aminomethyl)thiophene-3-carboxylic acid
-
pH 8.5, 25C
-
0.077
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: pyruvate
0.099
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: glyoxylate
0.135
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: glyoxylate
0.165
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: pyruvate
0.18
-
4-aminobutanoate
Q94FS9
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 30C
0.34
-
4-aminobutanoate
Q94FS9
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 30C
0.4
-
4-aminobutanoate
-
-
0.79
-
4-aminobutanoate
-
pH 8.5
0.79
-
4-aminobutanoate
-
pH 8.6, 25C
1.1
-
4-aminobutanoate
-
37C, pH 8.0
1.1
-
4-aminobutanoate
-
37C
1.1
-
4-aminobutanoate
-
-
1.2
-
4-aminobutanoate
-
pH 8.2
1.2
-
4-aminobutanoate
-
-
1.27
-
4-aminobutanoate
-
25C, pH 8.4
1.3
-
4-aminobutanoate
-
pH 8.5, 25C
1.7
-
4-aminobutanoate
-
pH 8.0, 37C
2.2
2.3
4-aminobutanoate
-
-
2.2
2.3
4-aminobutanoate
-
pH 8.5
2.2
2.3
4-aminobutanoate
Candida guilliermondii var. membranaefaciens
-
-
2.2
-
4-aminobutanoate
-
pH 8.6, temperature not specified in the publication
2.4
-
4-aminobutanoate
-
at 25C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol; pH 8.5
3.2
-
4-aminobutanoate
A5H0J5, A5H0J6, -
in 100 mM potassium phosphate (pH 8.0), 0.1 mM pyridoxal 5'-phosphate
3.3
4.8
4-aminobutanoate
-
-
3.3
4.8
4-aminobutanoate
-
pH 8.0, 37C
3.3
-
4-aminobutanoate
-
pH 8.0, 37C
4
-
4-aminobutanoate
-
38C, pH 8.5
4.7
-
4-aminobutanoate
-
mutant I50Q/G295Y, 25C, pH 7.8
5.8
-
4-aminobutanoate
-
wild-type, 25C, pH 7.8
5.9
-
4-aminobutanoate
-
mutant E211S/I50G/C77K, 25C, pH 7.8
6.5
-
4-aminobutanoate
-
mitochondrial enzyme; pH 8.0
12.8
-
4-aminobutanoate
-
at pH 8.4 and 38C
30
-
4-aminobutanoate
-
mutant V241A, 25C, pH 7.8
53
-
4-aminobutanoate
-
synaptosomal enzyme, pH 8.0
68
-
4-aminobutanoate
-
mutant I50Q, 25C, pH 7.8
86
-
4-aminobutanoate
-
mutant E211S, 25C, pH 7.8
146
-
4-aminobutanoate
-
mutant E211S/I50H/V80T, 25C, pH 7.8
9.9
-
4-aminobutyrate
-, Q0K2K2
Km apparent value
0.014
-
4-Oxobutanoate
Q94FS9
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 30C
9.5
-
5-(aminomethyl)-1H-pyrrole-2-carboxylic acid
-
pH 8.5, 25C
-
2.49
-
5-(aminomethyl)furan-2-carboxylic acid
-
pH 8.5, 25C
-
6.3
-
5-(aminomethyl)thiophene-2-carboxylic acid
-
pH 8.5, 25C
-
0.1
-
alpha-ketoglutarate
-
pH 8.4, 25C
1.05
-
beta-Alanine
-
-
4.4
-
beta-Alanine
-
pH 8.0, 37C
7.6
-
beta-Alanine
A5H0J5, A5H0J6, -
pH 8.0, 30C
18
-
beta-Alanine
-
-
2.3
-
DL-3-amino-1-cyclopentene-1-carboxylic acid
-
-
3.2
-
gamma-aminobutanoate
A5H0J5, A5H0J6, -
pH 8.0, 30C
2.6
-
gamma-aminobutanoic acid
-
pH 8.5
0.0165
-
glyoxylate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
0.039
-
glyoxylate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
0.11
-
glyoxylate
Q94FS9
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 30C
2.72
-
L-3-aminoisobutanoate
-
-
2.4
-
L-alanine
Q94FS9
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 30C
2.5
-
putrescine
-
-
-
0.0188
-
pyruvate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
0.023
-
pyruvate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
0.14
-
pyruvate
Q94FS9
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 30C
0.24
-
pyruvate
-
pH 8.2
8
-
tetrazole-5-butanamine
-
at 25C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
2.3
-
tetrazole-5-ethanamine
-
at 25C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
2.4
-
tetrazole-5-propanamine
-
at 25C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
2.9
-
L-ornithine
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic study; pH-dependence of kinetic data
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.69
-
1H-tetrazole-5-butanamine
-
pH 8.5
0.26
-
1H-tetrazole-5-ethanamine
-
pH 8.5
0.48
-
1H-tetrazole-5-propanamine
-
pH 8.5
5.6e-05
-
4-(aminomethyl)-1H-pyrrole-2-carboxylic acid
-
pH 8.5, 25C
-
3.83e-05
-
4-(aminomethyl)furan-2-carboxylic acid
-
pH 8.5, 25C
-
1.38e-05
-
4-(aminomethyl)furan-3-carboxylic acid
-
pH 8.5, 25C
-
8.6e-05
-
4-(aminomethyl)thiophene-2-carboxylic acid
-
pH 8.5, 25C
-
0.00023
-
4-aminobutanoate
-
mutant E211S/I50H/V80D, 25C, pH 7.8
0.0005
-
4-aminobutanoate
-
mutant E211S/I50G/C77R, 25C, pH 7.8
0.003
-
4-aminobutanoate
-
mutant E211S/I50G, 25C, pH 7.8
0.004
-
4-aminobutanoate
-
mutant E211S/I50Q/G295Y/V241A, 25C, pH 7.8
0.0058
-
4-aminobutanoate
-
mutant E211S/I50N/V80T, 25C, pH 7.8
0.0075
-
4-aminobutanoate
-
mutant E211S/I50N/V80D, 25C, pH 7.8
0.028
-
4-aminobutanoate
-
mutant I50Q/G295Y, 25C, pH 7.8
0.106
-
4-aminobutanoate
-
mutant E211S/I50H/V80T, 25C, pH 7.8
0.25
-
4-aminobutanoate
-
mutant E211S/I50G/C77K, 25C, pH 7.8
0.56
-
4-aminobutanoate
-
mutant E211S, 25C, pH 7.8
0.81
-
4-aminobutanoate
-
pH 8.5
0.81
-
4-aminobutanoate
-
pH 8.5, 25C
0.817
-
4-aminobutanoate
-
at 25C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
0.84
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: pyruvate
1
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: glyoxylate
1.93
-
4-aminobutanoate
-
mutant V241A, 25C, pH 7.8
2.6
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: pyruvate
2.7
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: glyoxylate
6.9
-
4-aminobutanoate
Q94FS9
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 30C
10.6
-
4-aminobutanoate
Q94FS9
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 30C
13.2
-
4-aminobutanoate
-
-
13.5
-
4-aminobutanoate
-
mutant I50Q, 25C, pH 7.8
47.4
-
4-aminobutanoate
-
wild-type, 25C, pH 7.8
10.8
-
4-Oxobutanoate
Q94FS9
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 30C
2.5e-05
-
5-(aminomethyl)-1H-pyrrole-2-carboxylic acid
-
pH 8.5, 25C
-
0.00056
-
5-(aminomethyl)furan-2-carboxylic acid
-
pH 8.5, 25C
-
0.00016
-
5-(aminomethyl)thiophene-2-carboxylic acid
-
pH 8.5, 25C
-
0.74
-
glyoxylate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
2.6
-
glyoxylate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
9.7
-
glyoxylate
Q94FS9
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 30C
15.4
-
L-alanine
Q94FS9
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 30C
0.8
-
pyruvate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
2.7
-
pyruvate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
10.6
-
pyruvate
Q94FS9
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 30C
0.693
-
tetrazole-5-butanamine
-
at 25C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
0.265
-
tetrazole-5-ethanamine
-
at 25C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
0.477
-
tetrazole-5-propanamine
-
at 25C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10.4
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: glyoxylate
4334
10.9
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: pyruvate
4334
16.1
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: pyruvate
4334
19.5
-
4-aminobutanoate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: glyoxylate
4334
31
-
4-aminobutanoate
Q94FS9
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 30C
4334
39
-
4-aminobutanoate
Q94FS9
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 30C
4334
770
-
4-Oxobutanoate
Q94FS9
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 30C
4788
45.7
-
glyoxylate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
11154
66.6
-
glyoxylate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
11154
88
-
glyoxylate
Q94FS9
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 30C
11154
6.4
-
L-alanine
Q94FS9
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 30C
12048
42.7
-
pyruvate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
16065
76
-
pyruvate
Q94FS9
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 30C
16065
116
-
pyruvate
J9XGP8, J9XGZ5
pH 9, 25C, fixed substrate: 4-aminobutanoate
16065
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.364
-
(+/-)piperidine-3-sulfonic acid
-
mixed inhibition at 37C
0.052
-
(1R,4S)-4-amino-2-cyclopentene-1-carboxylic acid
-
-
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)
2.7
-
(1S,4R)-4-amino-2-cyclopentene-1-carboxylic acid
-
-
3.75
-
(1S,4S)-2-(difluoromethylidene)-4-(1H-tetrazol-5-yl)cyclopentanamine
-
pH 6.5
1.2
-
(4R)-4-amino-1-cyclopentene-1-carboxylic acid
-
-
72
-
(4S)-4-amino-1-cyclopentene-1-carboxylic acid
-
-
5.6
-
1H-tetrazole-5-(alpha-vinyl-propanamine)
-
pH 8.5
0.008
-
2,4-diaminobutanoate
-
synaptosomal enzyme, pH 8.0
0.013
-
2,4-diaminobutanoate
-
cytoplasmic enzyme, pH 8.0
0.434
-
2-Aminobenzenesulfonate
-
competitive inhibition at 37C
0.033
-
2-Aminobutanoate
Candida guilliermondii var. membranaefaciens
-
-
1.01
-
2-aminoethane phosphonic acid
-
competitive inhibition at 37C
0.598
-
2-N-(acetylamino)cyclohexane sulfonic acid
-
competitive inhibition at 37C
0.00018
-
2-oxoglutarate
-
38C, pH 8.5
0.013
-
3-Mercaptopropionic acid
-
-
1.59
-
4-(aminomethyl)-1H-pyrrole-2-carboxylic acid
-
pH 8.5, 25C
-
1.64
-
4-(aminomethyl)furan-2-carboxylic acid
-
pH 8.5, 25C
-
2.27
-
4-(aminomethyl)furan-3-carboxylic acid
-
pH 8.5, 25C
-
1.35
-
4-(aminomethyl)thiophene-2-carboxylic acid
-
pH 8.5, 25C
-
2.86
-
4-(aminomethyl)thiophene-3-carboxylic acid
-
pH 8.5, 25C
-
0.47
-
4-acryloylphenol
-
-
0.44
-
4-amino-2-fluorobutanoate
-
pH 8.6, 37C
2.6
-
4-aminohex-5-enoic acid
-
-
26
-
4-aminohex-5-enoic acid
-
pH 8.6, 25C
2.14
-
5-(aminomethyl)-1H-pyrrole-2-carboxylic acid
-
pH 8.5, 25C
-
1.4
-
5-(aminomethyl)furan-2-carboxylic acid
-
pH 8.5, 25C
-
2.49
-
5-(aminomethyl)thiophene-2-carboxylic acid
-
pH 8.5, 25C
-
0.039
-
alpha-alanine
Candida guilliermondii var. membranaefaciens
-
-
0.24
-
Aminooxyacetate
-
-
0.62
-
Aminooxyacetate
-
wild-type, pH 7.8, 25C
1.13
-
Aminooxyacetate
-
mutant V241A, pH 7.8, 25C
3.7
-
ATP
-
-
0.0355
-
beta-Alanine
Candida guilliermondii var. membranaefaciens
-
-
0.55
-
beta-Alanine
Q94FS9
-
0.002
-
Butyric acid
Candida guilliermondii var. membranaefaciens
-
-
0.6
-
DL-3-amino-1-cyclopentene-1-carboxylic acid
-
-
38
-
DL-trans-4-amino-2-cyclopentene-1-carboxylic acid
-
-
0.0044
-
ethanolamine O-sulfate
-
37C, pH 8.4
68
-
ethylamine-2-sulfonic acid
-
pH 8.6, 25C
19
-
Glutarate
-
wild-type, pH 7.8, 25C
140
-
Glutarate
-
mutant V241A, pH 7.8, 25C
233
-
Glutarate
-
mutant I50Q, pH 7.8, 25C
3.7
-
glycine
Q94FS9
-
3.9
-
Maleate
-
wild-type, pH 7.8, 25C
-
46
-
Maleate
-
mutant I50Q, pH 7.8, 25C
-
780
-
Maleate
-
mutant V241A, pH 7.8, 25C
-
0.46
-
ornithine
Q94FS9
-
0.003
-
Propionic acid
Candida guilliermondii var. membranaefaciens
-
-
27
-
succinate
-
wild-type, pH 7.8, 25C
197
-
succinate
-
mutant I50Q, pH 7.8, 25C
720
-
succinate
-
mutant V241A, pH 7.8, 25C
0.0066
-
Succinic semialdehyde
-
38C, pH 8.5
5.6
-
tetrazole-5-(alpha-vinyl-propanamine)
-
-
0.32
-
vigabatrin
-
competitive inhibition at 37C
0.62
-
vigabatrin
Q94FS9
-
1
-
vigabatrin
-
pH 8.4, 25C
2.6
-
vigabatrin
-
pH 8.5
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00399
-
3-chloro-1-(4-hydroxyphenyl)propan-1-one
-
-
0.0165
-
4-hydroxybenzaldehyde
-
IC50: 0.0165 mM, competitive inhibition
0.0165
-
4-hydroxybenzaldehyde
-
-
0.0154
-
4-hydroxybenzylamine
-
IC50: 0.0154 mM, competitive inhibition
0.0018
-
gabaculine
-
IC50: 0.0018 mM, potent and irreversible inhibitor
0.35
-
vigabatrin
-
IC50: 0.35 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0183
-
Q84P52, Q84P53, Q84P54, -
isoform GABA-T2, using pyruvate as amino cceptor
0.0209
-
Q84P52, Q84P53, Q84P54, -
isoform GABA-T2, using glyoxylate as amino cceptor
0.1
-
A5H0J5, A5H0J6, -
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30C
0.13
-
A5H0J5, A5H0J6, -
substrate beta-alanine, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
0.14
-
O13837, -
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30C
0.15
-
P17649
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30C
0.1785
-
Q84P52, Q84P53, Q84P54, -
isoform GABA-T3, using glyoxylate as amino acceptor
0.2065
-
Q84P52, Q84P53, Q84P54, -
isoform GABA-T3, using pyruvate as amino acceptor
0.75
-
A5H0J5, A5H0J6, -
substrate gamma-aminobutanoate, continuous assay with succinate dehydrogenase, pH 8.0, 30C
0.89
-
-
pH 8.5
1.6
-
A5H0J5, A5H0J6, -
substrate gamma-aminobutanoate, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
1.8
3.5
-
37C
2.5
-
-
38C, pH 8.6
3.495
-
Q84P52, Q84P53, Q84P54, -
isoform GABA-T1, using glyoxylate as amino acceptor
3.52
-
A5H0J5, A5H0J6, -
substrate beta-alanine, discontinuous determination of glutamate using glutamate dehydrogenase in the presence of 10 M hydrazine, pH 8.0, 30C
3.6
-
P17649
substrate gamma-aminobutanoate, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
3.67
-
O13837, -
continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
4.1
-
-
-
4.5
-
A5H0J5, A5H0J6, -
substrate beta-alanine, continuous assay using malonic semialdehyde decarboxylase and alcohol dehydrogenase, pH 8.0, 30C
4.9
-
-
-
4.9
-
-
38C, pH 8.6
5
-
-
37C, pH 8.0
5.79
-
Q84P52, Q84P53, Q84P54, -
isoform GABA-T1, using pyruvate as amino acceptor
10
-
-
38C, pH 8.5
12.8
-
A5H0J5, A5H0J6, -
substrate gamma-aminobutanoate, continuous assay with succinate dehydrogenase, pH 8.0, 30C; using 4-aminobutanoate as substrate
17.5
-
-
pH 8.4, 25C
18
-
-
pH 8.4, 25C
18.2
-
-
-
46.8
-
-
-
52.33
-
Candida guilliermondii var. membranaefaciens
-
-
170
-
-
pH 7.3, 37C, liver enzyme
260
-
-
pH 7.3, 37C, kidney enzyme
600
-
-
pH 7.3, 37C, brain enzyme
1736
-
Q71SH3
pH 8.2, 30C
additional information
-
-
stable-isotope dilution assay
additional information
-
-
3.4 units/mg in crude brain homogenate and 51.2 units/mg after 15fold purification
additional information
-
-, Q0K2K2
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8
-
mitochondrial enzyme
7
-
-
mitochondrial enzyme
7.8
8
Candida guilliermondii var. membranaefaciens
-
at 35C
8
-
-
synaptosomal enzyme
8
-
Q71SH3
-
8
-
A5H0J5, A5H0J6, -
-
8.1
-
-
-
8.5
-
-
-
8.5
-
-
assay at
8.6
-
-
-
8.6
-
-
assay at
8.7
-
-
-
8.7
-
-
isozyme II
8.8
-
-
isozyme I
9
-
-, Q0K2K2
-
9
-
Q94FS9
for pyruvate-dependent GABA-T activity
9
-
J9XGP8, J9XGZ5
assay at; assay at
additional information
-
-
pI: 5.9
additional information
-
-
pI: 5.9 and 6.35 (isozyme II), pI: 6.1 and 6.3 (isozyme I)
additional information
-
-
pI: 6.8
additional information
-
-
pI: 5.5
additional information
-
-
pI: 6.7
additional information
-
Candida guilliermondii var. membranaefaciens
-
pI: 5.7
additional information
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
no activity below
6.5
11
-
no activity above or below
6.9
8.8
-
about half-maximal activity at pH 6.9 and 8.8
7
9
A5H0J5, A5H0J6, -
more than 70% of maximum activity
7.2
10
-, Q0K2K2
enzyme activity is detected
7.4
9
-
about half-maximal activity at pH 7.4 and about 90% of maximal activity at pH 9
8
9.2
-
about 50% of maximal activity at pH 9.2; about half-maximal activity at pH 8
8
9.2
-
about 60% of maximal activity at pH 9.2; about half-maximal activity at pH 8
8.5
10
Q94FS9
-
8.5
9.5
J9XGP8, J9XGZ5
maximal activity; maximal activity
11
-
-
and above, no activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
J9XGP8, J9XGZ5
assay at; assay at
30
-
Q71SH3
-
45
-
Candida guilliermondii var. membranaefaciens
-
-
50
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
40
-
about half-maximal activity at 20C and 40C
20
50
-
linear increase, above 55C rapid decrease
25
45
Candida guilliermondii var. membranaefaciens
-
linear increase, above 45C rapid decrease
30
55
-
about half-maximal activity at 30C and 55C
30
60
-
linear increase, above 65C rapid decrease
35
70
-
about half-maximal activity at 35C and 70C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.97
-
-
calculated from sequence of cDNA
6.33
-
Q71SH3
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
immunohistochemical study on distribution
Manually annotated by BRENDA team
-, Q2PZI2
; 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
Manually annotated by BRENDA team
Q84P52, Q84P53, Q84P54, -
-
Manually annotated by BRENDA team
-
20% of the activity in grey matter
Manually annotated by BRENDA team
Q84P52, Q84P53, Q84P54, -
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
Manually annotated by BRENDA team
-, Q2PZI2
; enzyme activity of gamma-aminobutanoate transaminase is highest in the hypothalamus and optic textum
Manually annotated by BRENDA team
Q71SH3
induction during leaf senescence with highest level at the S3 senescent stage
Manually annotated by BRENDA team
-
infected with blast fungus Magnaporthe grisea
Manually annotated by BRENDA team
Q84P52, Q84P53, Q84P54, -
-
Manually annotated by BRENDA team
-, Q2PZI2
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
Manually annotated by BRENDA team
-, Q2PZI2
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
Manually annotated by BRENDA team
Q84P52, Q84P53, Q84P54, -
-
Manually annotated by BRENDA team
-, Q2PZI2
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
Manually annotated by BRENDA team
-
retinal tissue of albino mice treated with two vigabatrin doses
Manually annotated by BRENDA team
Q84P52, Q84P53, Q84P54, -
-
Manually annotated by BRENDA team
Q84P52, Q84P53, Q84P54, -
-
Manually annotated by BRENDA team
Q84P52, Q84P53, Q84P54, -
-
Manually annotated by BRENDA team
-, Q2PZI2
enzyme activity of gamma-aminobutanoate transaminase is highest in the hypothalamus and optic tectum
Manually annotated by BRENDA team
-, Q2PZI2
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
Manually annotated by BRENDA team
-
biochemical and histochemical data to distribution, young to elderly men
Manually annotated by BRENDA team
-
mostly arteries and partly veins of, strong decrease of activity with age
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Candida guilliermondii var. membranaefaciens
-
-
Manually annotated by BRENDA team
Candida guilliermondii var. membranaefaciens Y43
-
-
-
Manually annotated by BRENDA team
Q84P52, Q84P53, Q84P54, -
isoform GABA-T1
Manually annotated by BRENDA team
Euglena gracilis mutant, Nicotiana tabacum Samsun N.N.
-
-
-
Manually annotated by BRENDA team
Pseudomonas sp. F-126
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Arthrobacter aurescens (strain TC1)
Arthrobacter aurescens (strain TC1)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
-
-, Q0K2K2
denaturated protein, determined by SDS-PAGE
53060
-
-
calculated from sequence of cDNA
54200
-
J9XGP8, J9XGZ5
SDS-PAGE, single recombinant truncated MdGABA-T; SDS-PAGE, single recombinant truncated MdGABA-T
97000
-
-
gel filtration
98000
-
A5H0J5, A5H0J6, -
PAGE
100000
-
-
gel filtration
100000
-
-
SDS-PAGE, absence of 2-mercaptoethanol
103000
-
-
PAGE
105000
-
-
gel filtration
105000
-
-
-
105000
-
-
gel filtration
107000
-
-
calculated from amino acid composition
107000
-
Candida guilliermondii var. membranaefaciens
-
gel filtration
109000
-
-
high speed sedimentation equilibrium centrifugation
110000
-
-
liver enzyme, gel filtration
110100
-
-
liver enzyme, crystallographic data
111000
-
A5H0J5, A5H0J6, -
PAGE
120000
-
-, Q0K2K2
mass of native protein, determined by gel filtration
176000
178000
-
gel filtration, sedimentation equilibrium centrifugation
200000
-
-
sucrose density gradient centrifugation
additional information
-
-
compared to liver enzyme, mature form of brain enzyme has an additional peptide at the N-terminus which may be cleaved by liver mitochondrial extract
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 52000, SDS-PAGE, x * 53950, deduced from gene sequence
?
-
x * 50000, SDS-PAGE
?
Q71SH3
x * 56474, recombinant protein, calculated
dimer
-
1 * 53000 + 1 * 58000, SDS-PAGE
dimer
-
brain enzyme, SDS- or SDS/urea-PAGE
dimer
-
2 * 55000, liver enzyme, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE with or without DTT or urea
dimer
-
2 * 50000, SDS-PAGE
dimer
-
alpha2, liver enzyme, crystallization data
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 53300, SDS-PAGE, brain enzyme, 2 * 52700, SDS-PAGE, liver enzyme
dimer
-
2 * 50000, SDS-PAGE, presence of 2-mercaptoethanol
dimer
A5H0J5, A5H0J6, -
2 * 56000, SDS-PAGE; 2 * 56000, SDS-PAGE
homodimer
-, Q0K2K2
gel filtration
additional information
-
amino acid composition
additional information
-
crosslinking with bifunctional sulfhydryl reagent DMDS at one mol per enzyme dimer
additional information
-
three different enzyme species isolated are not isozymes but products of proteolysis differing by 3,7,12 residues, Na2EDTA inhibits N-terminal cleavage during preparation
additional information
Q71SH3
contains a putative mitochondrial targeting sequence and a conserved sequence of pyridoxal 5-phosphate binding domain
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with inhibitor aminooxyacetate
-
mutant I50Q, V241A, E211S
-
docking calculations for substrates 3-(aminomethyl)benzoic acid, [3-(aminomethyl)phenyl]acetic acid and [2-(aminomethyl)phenyl]acetic acid, using the crystallographic structure of the enzyme in complex with vigabatrin
-
in complex with mechanism-based inhibitor (1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid
-
native form and in complex with inhibitor vigabatrin and with 4-ethynyl-4-aminobutanoate
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
10
-
15 min stable, 37C
6
10
-
15 min stable, 37C
6.5
7.5
-
below and above, rapid inactivation
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
t1/2: 3 h
37
-
-
15 min stable, pH 6-10
42
-
Candida guilliermondii var. membranaefaciens
-
up to, at least 10 min stable
45
-
-
up to, at least 10 min stable, pH 8
46
-
Candida guilliermondii var. membranaefaciens
-
up to, at least 10 min stable in the presence of pyridoxal phosphate
50
60
-
slow decrease of activity, rapid inactivation above 60C
50
-
-
3 h, 80% loss of activity
50
-
Candida guilliermondii var. membranaefaciens
-
up to, at least 10 min stable in the presence of 2-oxoglutarate
50
-
-
above, 10 min, inactivation; up to, stable
50
-
Q71SH3
10 min, 20% residual activity
55
-
-
slow inactivation
55
-
-
rapid inactivation
55
-
-
3 h, inactivation
60
-
-
up to, at least 15 min stable, pH 8
60
-
-
10 min stable in the presence of pyridoxal phosphate
65
-
-
above, 15 min, inactivation
70
-
-
15 min stable in the presence of pyridoxal phosphate
additional information
-
Candida guilliermondii var. membranaefaciens
-
2-oxoglutarate protects against heat inactivation, better than pyridoxal phosphate
additional information
-
-
pyridoxal phosphate protects against heat inactivation
additional information
-
-
pyridoxal phosphate protects against heat inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-oxoglutarate protects against heat inactivation, better than pyridoxal phosphate
Candida guilliermondii var. membranaefaciens
-
freeze-thawing slightly inactivates
-
pyridoxal phosphate protects against heat inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 12 days, 57% residual activity
-
-20C, protected with 2-aminoethylisothiouronium bromide hydrobromide and pyridoxal phosphate, several months
-
-20C, several months
-
4C, 12 days, 57% residual activity
P17649
4C, 12 days, 57% residual activity
O13837, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ProBond nickel resin column chromatography
Q94FS9
-
Candida guilliermondii var. membranaefaciens
-
by anion exchange chromatography
-, Q0K2K2
nickel-chelating Sepharose chromatography and Sepharose S12 gel filtration
A5H0J5, A5H0J6, -
partial
-
-
Q84P52, Q84P53, Q84P54, -
cationic (I) and anionic (II) form
-
expressed in E. coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
co-expression of the truncated GABA-T cDNA with the GroES/ELmolecular chaperone complex in Escherichia coli BL-21(DE3) Rosetta (pLysS) cells, and GABA-T is expressed in Nicotiana tabacum BY-2 cells
Q94FS9
expressed in Escherichia coli BL-21(DE3) cells; expression as His-tagged protein; expression as His-tagged protein
A5H0J5, A5H0J6, -
removal of the N-terminal targeting presequences yields good recovery of the soluble recombinant proteins in Escherichia coli when they are co-expressed with the GroES/EL molecular chaperone complex; removal of the N-terminal targeting presequences yields good recovery of the soluble recombinant proteins in Escherichia coli when they are co-expressed with the GroES/EL molecular chaperone complex
J9XGP8, J9XGZ5
expressed in Escherichia coli strain XL1-Blue
-
expression as His-tagged protein
P17649
expression as His-tagged protein
O13837, -
full-length GABA-T1 isoform fused to the green fluorescent protein is expressed in Nicotiana tabacum, and GABA-T1 isoform is co-expressed with the GroES/EL molecular chaperone complex in Escherichia coli BL-21(DE3) Rosetta (pLysS) cells; full-length GABA-T2 isoform fused to the green fluorescent protein is expressed in Nicotiana tabacum, and GABA-T2 isoform is co-expressed with the GroES/EL molecular chaperone complex in Escherichia coli BL-21(DE3) Rosetta (pLysS) cells; full-length GABA-T3 isoform fused to the green fluorescent protein is expressed in Nicotiana tabacum, and GABA-T3 isoform is co-expressed with the GroES/EL molecular chaperone complex in Escherichia coli BL-21(DE3) Rosetta (pLysS) cells
Q84P52, Q84P53, Q84P54, -
brain cDNA, expressed in Escherichia coli strain BL21(DE3)pLysS transformed with expression vector pETG1.5
-
cDNA clone isolation and sequence determination
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression is highest in roots and increases as a function of leaf development
Q94FS9
transcript is detected inducibly in both homotaurine and GABA-grown cells
-, Q0K2K2
when beta-hydroxybutyrate (10 mM) is added to culture medium, GABA-transaminase mRNA expression is significantly suppressed in time- and dose-dependent manners, GABA-T enzymatic activity in beta-hydroxybutyrate-treated astrocytes is also suppressed, in accordance with its gene expression
P50554
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
additional information
-
mutants of GABA transaminase suppress the severe phenotype of succinic semialdehyde dehydrogenase mutants in Arabidopsis
additional information
-
the GABA transaminase loss-of-function mutant pop2-1 is oversensitive to ionic stress but not to osmotic stress
K330R
-
no catalytic activity, no pyridoxal 5'-phosphate covalently linked to protein
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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
apoenzyme reconstituted with exogenous pyridoxal 5-phosphate almost completely regains catalytic activity
-
enzyme inhibited by 6-azauracil is reactivated by dialysis but not by addititon of pyridoxal 5'-phosphate
-
after inhibition by carbonyl reagents or sulfhydryl reagents enzyme may be reactivated by incubation with pyridoxal 5-phosphate or thiol reagents
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
chronical administration of vigabatrin with drinking water completely and reversibly eliminates the psychophysical evidence of tinnitus