Any feedback?
Information on EC 2.6.1.19 - 4-aminobutyrate-2-oxoglutarate transaminase and Organism(s) Sus scrofa and UniProt Accession P80147
for references in articles please use BRENDA:EC2.6.1.19Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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. cf. EC 2.6.1.120, beta-alanine---2-oxoglutarate transaminase.
Specify your search results
Word Map
- 2.6.1.19
-
gabaergic
-
neurotransmitter
- seizure
- epilepsy
-
anticonvulsant
- agonist
-
antiepileptic
-
aminooxyacetic
-
gamma-vinyl
- dopamine
- bicuculline
- muscimol
-
shunt
- hypothalamus
-
neurotransmission
- pyridoxal
-
gabab
- convulsion
- valproate
- gabaculine
-
excitatory
- baclofen
- striatum
- benzodiazepine
-
transmitter
-
synaptosomes
- diazepam
-
transamination
- ssadh
-
gaba-mediated
-
substantia
- picrotoxin
-
neurochemical
-
tiagabine
-
pentylenetetrazol
-
3hgaba
-
3-mercaptopropionic
-
4.1.1.15
- homocarnosine
- gamma-hydroxybutyrate
-
silverman
-
nipecotic
- gabapentin
-
plp-dependent
-
kindling
-
electroshock
-
enzyme-activated
-
clonic
-
gaba-induced
-
ethosuximide
- medicine
- molecular biology
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
gaba-t, gaba transaminase, gaba-transaminase, gaba-at, 4-aminobutyrate aminotransferase, gaba aminotransferase, gamma-aminobutyric acid transaminase, gabat, gamma-aminobutyric acid aminotransferase, gamma-aminobutyrate transaminase, 
more
topSYNONYM 
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
-
-
-
-
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
-
-
-
-
GABA aminotransferase
-
-
-
-
GABA transaminase
-
-
-
-
gamma-aminobutyrate transaminase
-
-
-
-
gamma-aminobutyric acid aminotransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
catalytic mechanism of GABA-AT for degradation of GABA into succinic semialdehyde, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -
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. cf. EC 2.6.1.120, beta-alanine---2-oxoglutarate transaminase.
CAS REGISTRY NUMBER
COMMENTARY
9037-67-6
-
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
(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
-
-
?
3-(aminomethyl)benzoic acid + 2-oxoglutarate
3-(iminomethyl)benzoic acid + L-glutamate
3.4% of the activity with 4-aminobutanoate
-
-
?
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + L-glutamate
-
-
-
?
[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
-
-
?
(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
-
-
?
(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
-
-
-
-
?
DL-3-amino-1-cyclopentene-1-carboxylic acid + 2-oxoglutarate
3-oxo-1-cyclopentene-1-carboxylic acid + L-glutamate
-
analogue of 4-aminobutanoate, vigabatrin
-
-
?
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
-
key-reaction of gamma-aminobutyrate(GABA)-shunt or bypass
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
involved in beta-alanine metabolism
-
-
?
5-aminopentanoate + 2-oxoglutarate
L-glutamate + 5-oxopentanoate
-
transamination at 85% the rate of 4-aminobutanoate
-
-
?
beta-alanine + 2-oxoglutarate
malonic semialdehyde + L-glutamate
-
effective amino group 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
-
transamination at 20% the rate of 4-aminobutanoate
-
-
r
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
4-aminobutanoate + 2-oxoglutarate
succinate semialdehyde + 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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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)-3-amino-4-difluoromethylenyl-1-cyclopentanoic acid
i.e. CPP-115, high inhibition of GABA-AT. Potential mechanism of inactivation of GABA-AT by CPP-115, overview. CPP-115 has been designed to inactivate GABA-AT via a Michael addition mechanism that would lead to a covalent adduct with the enzyme, similar to that with vigabatrin. But it is discovered from the crystal structure of GABAAT inactivated by CPP-115 that the enzyme forms a noncovalent, tightly bound complex with CPP-115 via strong electrostatic interactions between the two carboxylate groups in the resulting metabolite with Arg192 and Arg445 in the active site. Inactivation is initiated by Schiff base formation between CPP-115 and the lysine-bound PLP, followed by gamma-proton removal and tautomerization, resulting in a highly reactive Michael acceptor. Before Lys329 can attack this Michael acceptor, catalytic hydrolysis of the difluoromethylenyl group occurs, leading to the PLP-bound dicarboxylate metabolite, which elicits a conformational change in the enzyme and tightly binds to Arg192 and Arg445 via electrostatic interactions. Molecular dynamic simulations and computer modeling indicate a movement of the difluoromethylenyl group of the Michael acceptor away from Lys329 upon enzyme-catalyzed tautomerization, leaving it too far away from Lys329 for nucleophilic attack. The enzyme catalyzes its hydrolysis instead
(R,S)-4-amino-3-fluorobutanoic acid
the (R)-enantiomer inhibits the transamination of gamma-aminobutanoic acid 10 times more effectively than the (S)-enantiomer. On binding of free 4-amino-3-fluorobutanoic acid to enzyme the optimal conformation places the C-NH3 + and C-F bonds gauche in the (R)-enantiomer but anti in the (S)-enantiomer
(S)-3-amino-4-(difluoromethylenyl)cyclopent-1-ene-1-carboxylic acid
a highly potent gamma-aminobutyric acid aminotransferase inactivator for the treatment of addiction, design, synthesis method and mechanism, overview. Enzyme-bound structure analysis shows binding between the enzyme and a stable PLP-inhibitor noncovalent complex, rather than covalent modification, tautomeric forms of the structure of inhibitor-inactivated GABA-AT (eight theoretical tautomers of inhibitor-inactivated GABA-AT)
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
(+/-)-(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,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,4R)-4-amino-2-cyclopentene-1-carboxylic acid
-
analogue of 4-aminobutanoate, vigabatrin
(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
(S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid
-
mechanism-based inactivator, reacts via aromatization mechanism
cis-3-aminocyclohex-4-ene-1-carboxylic acid
-
conformationally rigid analogue of vigabatrin, mechanism
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
additional information
a series of gamma-aminobutyric acid (GABA) derivatives obtained from 4-(1,3-dioxoisoindolin-2-yl)butanoic acid are synthesized and analyzed as inhibitory ligands docking against human ABAT as well as pig ABAT receptors. Active site docking study, overview
-
additional information
molecular dynamics simulations, design of mechanism-based inhibitors, drug design, overview
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
2.4
4-aminobutanoate
-
at 25°C in 50 mM potassium diphosphate buffer, pH 8.5, containing 2 mM beta-mercaptoethanol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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)
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.7
additional information
additional information
-
pI: 5.9 and 6.35 (isozyme II), pI: 6.1 and 6.3 (isozyme I)
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
inhibition of GABA aminotransferase (GABA-AT), the enzyme that degrades GABA, is a possible strategy for the treatment of substance abuse. The raised GABA levels that occur as a consequence of the inhibition antagonize the rapid release of dopamine in the ventral striatum (nucleus accumbens) that follows an acute challenge by an addictive substance. In addition, increased GABA levels are also known to elicit an anticonvulsant effect in patients with epilepsy
physiological function
gamma-aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the central nervous system. The enzyme GABA aminotransferase (GABA-AT) degrades GABA
additional information
homology structure modeling using pig ABAT as template (PDB ID 6B6G)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GABT_PIG
500
0
56620
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
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
-
crosslinking with bifunctional sulfhydryl reagent DMDS at one mol per enzyme dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of enzyme inactivated by inhibitors (1S,2S,3E)-2-amino-3-(fluoromethylidene)cyclopentanecarboxylic acid and (1S,2S,3Z)-2-amino-3-(fluoromethylidene)cyclopentanecarboxylic acid. The Arg445-Glu270 salt bridge in the active site is disrupted during inactivation, and Glu270 rotates away from its original position to accommodate a weak electrostatic or hydrogen-bonding interaction between the formyl group of a metabolite and Arg445
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
enzyme bound to inhibitor (S)-3-amino-4-(difluoromethylenyl)cyclopent-1-ene-1-carboxylic acid, X-ray diffraction structure determination and analysis at 1.95 A resolution
native form and in complex with inhibitor vigabatrin and with 4-ethynyl-4-aminobutanoate
in complex with mechanism-based inhibitor (1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
brain cDNA, expressed in Escherichia coli strain BL21(DE3)pLysS transformed with expression vector pETG1.5
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Choi, S.Y.; Kim, D.S.
Catalytic and structural properties of 4-aminobutyrate aminotransferase
Han'guk Saenghwa Hak Hoe Chi
24
508-514
1991
Sus scrofa
-
Bloch-Tardy, M.; Rolland, B.; Gonnard, P.
Pig brain 4-aminobutyrate 2-ketoglutarate transaminase. Purification, kinetics and physical properties
Biochimie
56
823-832
1974
Sus scrofa
Cooper, A.J.L.
Glutamate-gamma-aminobutyrate transaminase
Methods Enzymol.
113
80-82
1985
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Buzenet, A.M.; Fages, C.; Bloch-Tardy, M.; Gonnard, P.
Purification and properties of 4-aminobutyrate 2-ketoglutarate aminotransferase from pig liver
Biochim. Biophys. Acta
522
400-411
1978
Sus scrofa
Markovic-Housley, Z.; Schirmer, T.; Fol, B.; Jansonius, J.N.; De Biase, D.; John, R.A.
Crystallization and preliminary X-ray analysis of gamma-aminobutyric acid transaminase
J. Mol. Biol.
214
821-823
1990
Sus scrofa
Kwon, O.S.; Park, J.; Churchich, J.E.
Brain 4-aminobutyrate aminotransferase. Isolation and sequence of a cDNA encoding the enzyme
J. Biol. Chem.
267
7215-7216
1992
Sus scrofa
Park, J.; Osei, Y.D.; Churchich, J.E.
Isolation and characterization of recombinant mitochondrial 4-aminobutyrate aminotransferase
J. Biol. Chem.
268
7636-7639
1993
Sus scrofa
Sung, B.K.; Kim, Y.T.
Structural arrangement for functional requirements of brain recombinant 4-aminobutyrate aminotransferase
J. Biochem. Mol. Biol.
33
43-48
2000
Sus scrofa
-
Fu, M.; Nikolic, D.; Van Breemen, R.B.; Silverman, R.B.
Mechanism of inactivation of gamma-aminobutyric acid aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid
J. Am. Chem. Soc.
121
7751-7759
1999
Sus scrofa
-
Choi, S.; Storici, P.; Schirmer, T.; Silverman, R.B.
Design of a conformationally restricted analogue of the antiepilepsy drug Vigabatrin that directs its mechanism of inactivation of gamma-aminobutyric acid aminotransferase
J. Am. Chem. Soc.
124
1620-1624
2002
Sus scrofa
Storici, P.; Capitani, G.; De Biase, D.; Moser, M.; John, R.A.; Jansonius, J.N.; Schirmer, T.
Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy
Biochemistry
38
8628-8634
1999
Sus scrofa
Qiu, J.; Pingsterhaus, J.M.; Silverman, R.B.
Inhibition and substrate activity of conformationally rigid vigabatrin analogues with gamma-aminobutyric acid aminotransferase
J. Med. Chem.
42
4725-4728
1999
Sus scrofa
Koo, Y.K.; Nandi, D.; Silverman, R.B.
The multiple active enzyme species of gamma-aminobutyric acid aminotransferase are not isozymes
Arch. Biochem. Biophys.
374
248-254
2000
Sus scrofa
Kim, Y.T.; Song, Y.H.; Churchich, J.E.
Recombinant brain 4-aminobutyrate aminotransferases overexpression, purification, and identification of Lys-330 at the active site
Biochim. Biophys. Acta
1337
248-256
1997
Sus scrofa
Sung, B.K.; Cho, J.J.; Kim, Y.T.
Functional expression and characterization of C-terminal mutant of 4-aminobutyrate aminotransferase
J. Biochem. Mol. Biol.
32
181-188
1999
Sus scrofa
-
Storici, P.; Qiu, J.; Schirmer, T.; Silverman, R.B.
Mechanistic crystallography. Mechanism of inactivation of gamma-aminobutyric acid aminotransferase by (1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid as elucidated by crystallography
Biochemistry
43
14057-14063
2004
Sus scrofa
Yuan, H.; Silverman, R.B.
New substrates and inhibitors of gamma-aminobutyric acid aminotransferase containing bioisosteres of the carboxylic acid group: Design, synthesis, and biological activity
Bioorg. Med. Chem.
14
1331-1338
2005
Sus scrofa
Storici, P.; De Biase, D.; Bossa, F.; Bruno, S.; Mozzarelli, A.; Peneff, C.; Silverman, R.B.; Schirmer, T.
Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin
J. Biol. Chem.
279
363-373
2004
Sus scrofa (P80147), Sus scrofa
Wang, Z.; Silverman, R.B.
Syntheses and evaluation of fluorinated conformationally restricted analogues of GABA as potential inhibitors of GABA aminotransferase
Bioorg. Med. Chem.
14
2242-2252
2006
Sus scrofa
Lu, H.; Silverman, R.B.
Fluorinated conformationally restricted gamma-aminobutyric acid aminotransferase inhibitors
J. Med. Chem.
49
7404-7412
2006
Sus scrofa
Henjum, S.; Hassel, B.
High-affinity GABA uptake and GABA-metabolizing enzymes in pig forebrain white matter: a quantitative study
Neurochem. Int.
50
365-370
2007
Sus scrofa
Clift, M.D.; Ji, H.; Deniau, G.P.; OHagan, D.; Silverman, R.B.
Enantiomers of 4-amino-3-fluorobutanoic acid as substrates for gamma-aminobutyric acid aminotransferase. Conformational probes for GABA binding
Biochemistry
46
13819-13828
2007
Sus scrofa (P80147)
Clift, M.D.; Silverman, R.B.
Synthesis and evaluation of novel aromatic substrates and competitive inhibitors of GABA aminotransferase
Bioorg. Med. Chem. Lett.
18
3122-3125
2008
Sus scrofa (P80147)
Hawker, D.D.; Silverman, R.B.
Synthesis and evaluation of novel heteroaromatic substrates of GABA aminotransferase
Bioorg. Med. Chem.
20
5763-5773
2012
Sus scrofa
Juncosa, J.I.; Groves, A.P.; Xia, G.; Silverman, R.B.
Probing the steric requirements of the gamma-aminobutyric acid aminotransferase active site with fluorinated analogues of vigabatrin
Bioorg. Med. Chem.
21
903-911
2013
Sus scrofa
Mathew, B.; Ahsan, M.
Molecular recognisation of 3a, 4-dihydro-3-H-indeno [1, 2-C] pyrazole-2-carboxamide/carbothioamide anticonvulsant analogues towards GABA-aminotransferase - an in silico approach
Cent. Nerv. Syst. Agents Med. Chem.
14
39-42
2014
Sus scrofa (P80147)
Lee, H.; Doud, E.H.; Wu, R.; Sanishvili, R.; Juncosa, J.I.; Liu, D.; Kelleher, N.L.; Silverman, R.B.
Mechanism of inactivation of gamma-aminobutyric acid aminotransferase by (1S,3S)-3-amino-4-difluoromethylene-1-cyclopentanoic acid (CPP-115)
J. Am. Chem. Soc.
137
2628-2640
2015
Sus scrofa (P80147)
Iftikhar, H.; Batool, S.; Deep, A.; Narasimhan, B.; Sharma, P.; Malhotra, M.
In silico analysis of the inhibitory activities of GABA derivatives on 4-aminobutyrate transaminase
Arab. J. Chem.
10
S1267-S1275
2017
Sus scrofa (P80147), Homo sapiens (P80404)
-
Juncosa, J.I.; Takaya, K.; Le, H.V.; Moschitto, M.J.; Weerawarna, P.M.; Mascarenhas, R.; Liu, D.; Dewey, S.L.; Silverman, R.B.
Design and mechanism of (S)-3-amino-4-(difluoromethylenyl)cyclopent-1-ene-1-carboxylic acid, a highly potent gamma-aminobutyric acid aminotransferase inactivator for the treatment of addiction
J. Am. Chem. Soc.
140
2151-2164
2018
Rattus norvegicus (P50554), Sus scrofa (P80147)
EXTERNAL LINKS (specific for EC-Number 2.6.1.19)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
