Information on EC 4.1.1.15 - glutamate decarboxylase

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

EC NUMBER
COMMENTARY hide
4.1.1.15
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RECOMMENDED NAME
GeneOntology No.
glutamate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamate = 4-aminobutanoate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
oxidative deamination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
GABA shunt
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L-glutamate degradation IV
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L-glutamate degradation IX (via 4-aminobutanoate)
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glutamate and glutamine metabolism
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Alanine, aspartate and glutamate metabolism
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beta-Alanine metabolism
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Taurine and hypotaurine metabolism
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Butanoate metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate 1-carboxy-lyase (4-aminobutanoate-forming)
A pyridoxal-phosphate protein. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-58-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
strain L. Heynh. Ecotype Columbia, 2 isoenzymes: GAD1 and GAD2
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene gadB
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Manually annotated by BRENDA team
gene gadB
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Manually annotated by BRENDA team
gene gad
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene gad
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
isolated from traditional Korean fermented food kimchi, gene gad
UniProt
Manually annotated by BRENDA team
LVIS_0079; gene gadB
UniProt
Manually annotated by BRENDA team
single gene gadB
UniProt
Manually annotated by BRENDA team
gene gadB
UniProt
Manually annotated by BRENDA team
gene gadBgene gadB
UniProt
Manually annotated by BRENDA team
gene gadBgene gadB
UniProt
Manually annotated by BRENDA team
male monkeys
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Manually annotated by BRENDA team
isoform GAD65
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Balb/c mice
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Manually annotated by BRENDA team
C57BL/6 mice
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Manually annotated by BRENDA team
spleen from Dasypus novemcinctus infected with Mycobacterium leprae
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Lactococcus lactis subsp. cremoris
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
gene PH0937
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Manually annotated by BRENDA team
and strain BB/OK
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Manually annotated by BRENDA team
gene gad
UniProt
Manually annotated by BRENDA team
serotypes Typhimurium and Enteritidis
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
ssp. thermophilus Y2, gene gadB
UniProt
Manually annotated by BRENDA team
gene gad
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
cv. Qidou 2
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
inbred line DH4866
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
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the 4-aminobutanoate shunt pathway possesses three enzymes encoded by genes gad, gabT, and gabD. Among the three, GAD is the key cytosolic-located enzyme which catalyzes the irreversible decarboxylation of L-glutamate to produce 4-aminobutanoate
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alpha-Methylglutamate
?
show the reaction diagram
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L-alpha-methylglutamate + O2
laevulinic acid + NH3
show the reaction diagram
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?
L-Asp
?
show the reaction diagram
L-Cysteic acid
?
show the reaction diagram
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-
-
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L-Cysteine sulfinic acid
?
show the reaction diagram
L-Glu
4-Aminobutanoate + CO2
show the reaction diagram
L-Glu
?
show the reaction diagram
L-glutamate
4-aminobutanoate + CO2
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Glu
4-Aminobutanoate + CO2
show the reaction diagram
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rate-limiting enzyme involved in the synthesis of gamma-aminobutyric acid
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?
L-Glu
?
show the reaction diagram
L-glutamate
4-aminobutanoate + CO2
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BaCl2
activates by 22% at 5 mM
CaCl2
potent activation
CoCl2
-
1 mM, activation to 128% of control
KBr
-
50 mM, enhances GAD activity in renal cortex homogenate
KCl
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50 mM, enhances GAD activity in renal cortex homogenate
LiCl
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50 mM, enhances GAD activity in renal cortex homogenate
Mn2+
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the optimal concentration (7.5 mM) of Mn2+ can also improve the activity of recombinant enzyme (164%), but the co-effect of Ca2+ and Mn2+ exhibits antagonism effect when added simultaneously
MnCl2
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1 mM, activation to 133% of control
NaBr
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50 mM, enhances GAD activity in renal cortex homogenate
NaCl
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50 mM, enhances GAD activity in renal cortex homogenate
NH4+
activates to 132% activity at 10 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
(E)-pent-2-enoic acid
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20% inhibition at 0.01 mg/ml
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
1-Methylimidazole
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about 85% residual activity at 5 mM, about 77% residual activity at 10 mM, about 65% residual activity at 20 mM
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
2,6-pyridine dicarboxylic acid
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2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
2-mercaptoethanol
2-Methyl-3,4-didehydroglutamic acid
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2-oxoglutarate
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
3,4,5-Trihydroxybenzoic acid
3,4-dihydroxybenzoic acid
3,4-dihydroxyphenylacetic acid
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3,5-Dihydroxybenzoic acid
3-Bromopyruvate
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3-Hydroxytyramine
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3-Mercaptopropionic acid
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
3-[(E)-(4-methoxybenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
4'-deoxypyridoxine-5'-phosphate
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about 60% inhibition of GAD65 at 3.5 mM, GAD67 is hardly affected
4'-O-methylpyridoxine-5'-phosphate
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decreases activity of GAD65 in unphysiologically high concentrations, about 60% inhibition at 3.5 mM. GAD67 activity is hardly affected
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
4,5-Dihydroxyisophthalic acid
4-(morpholin-4-yl)naphthalene-1,2-dione
4-(piperidin-1-yl)naphthalene-1,2-dione
4-aminobutanoate
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4-Aminohex-5-ynoic acid
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4-bromoisophthalic acid
4-methylimidazole
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about 75% residual activity at 5 mM, about 70% residual activity at 10 mM, about 58% residual activity at 20 mM
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
5,5'-dithiobis(2-nitrobenzoate)
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
acetate
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Ag+
58.3% residual activity at 2 mM
AgNO3
Al3+
91.2% residual activity at 2 mM
allylglycine
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Aminoethylylisothiouronium bromide
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aminooxyacetic acid
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Aminoxyacetate
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asiaticoside
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ATP
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in presence of leupeptin in freshly prepared homogenates. Inhibition of enzyme from homogenates stored without Triton X-100 for 24 h at 4°C
Avidin
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BaCl2
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1 mM, 78% inhibition
beta-Methylene-DL-Asp
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betulinic acid
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27% inhibition at 0.01 mg/ml
bilobalide
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biphenyl-3,3'-dicarbaldehyde
Ca2+
activates at 0.2 mM, slight inhibition above 1 mM
CaCl2
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1 mM, 31% inhibition
Carbohydrazide
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carboxymethoxylamine
CdCl2
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1 mM, 38% inhibition
CH3COOH
57.4% residual activity at 2 mM
Chelidamic acid
Chelidonic acid
Chloroacetamide
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no inhibition at pH 4.6, marked inhibition at pH 6.0 or higher
CoCl2
62% inhibition at 5mM
CuCl2
CuSO4
93% inhibition at 5mM
Cycloglutamates
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cyclosporin A
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up to 0.3 mM, partial inhibition of activity in homogenate, but not in the supernatant obtained after centrifuging the homogenate
Cys
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enzyme from embryos
D-erythro-4-fluoroglutamate
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D-Glu
dithiothreitol
DL-4-Amino-4-phosphonobutyrate
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DL-alpha-Aminoadipic acid
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DL-alpha-Methylglutamate
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DL-Penicillamine
FeCl3
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1 mM, 65% inhibition
FeSO4
92% inhibition at 5mM
ginsenosides
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23% inhibition at 0.01 mg/ml, ethanol extract of Panax quinquefolius, different glycoside derivatives, overview
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Glutamate gamma-hydroxamate
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weak
Glutarate
glutathione
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HgCl2
hydroxylamine
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isoniazide
isoniazide-induced seizures are mediated primarily through competition with the cofactor pyridoxal 5'-phosphate resulting in the inhibition of GAD activity
Isonicotinic acid hydrazide
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Isophthalic acid
L-Asn
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inhibits 4% at 1 mM
L-Asp
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inhibits 20% at 1 mM
L-aspartate beta-hydroxamate
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weak
L-cysteine
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L-Cysteine hydrochloride
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L-cysteine sulfinic acid
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L-erythro-4-fluoroglutamate
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L-Glu
L-Thiomalic acid
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malate
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weak
Mercaptosuccinic acid
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
MgCl2
-
1 mM, 46% inhibition
Mn2+
92.6% residual activity at 2 mM
MnSO4
88% inhibition at 5mM
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Na2SO4
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
oxaloacetate
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p-hydroxymercuribenzoate
Pb(CH3COO)2
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1 mM, 37% inhibition
PCMB
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0.1 mM, 68.5% inhibition at pH 4.6, irreversible
Phenylglyoxal
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reduced glutathione
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enzyme from embryos
Semicarbazide
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Substituted dicarboxylic acids
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Thiocarbohydrazide
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Thioglycollic acid
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Thiomalate
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Thiosemicarbazide
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ursolic acid
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; 11.2% inhibition at 0.01 mg/ml
valerenic acid
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20% inhibition at 0.01 mg/ml
Zinc acetate
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ZnCl2
ZnSO4
80.4% inhibition at 5mM
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
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activates
2-oxoglutarate
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stimulates
3-Mercaptopropionic acid
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5,5'-dithiobis(2-nitrobenzoic acid)
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stimulates
ADP
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2 mM, activation to about 170% of control without detergent. Activation to about 210% of control in presence of 1% Triton X-100
aminooxyacetic acid
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ammonium sulfate
at 1.8 M
AMP
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2 mM, activation to about 125% of control without detergent. Activation to about 140% of control in presence of 1% Triton X-100
apocalmodulin
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isoform GAD65, up to 60% activation, truncated isoform DAD67, up to 141% activation, no significant activation of GST-GAD67. Activation is due to an increase in affinity for cofactor pyridoxal 5'-phosphate
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asiaticoside
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20% activation at 0.01 mg/ml; an increase in GAD65 activity by 22% is observed with asiaticoside; an increase in GAD65 activity by 4.5% is observed with asiaticoside
ATP
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2 mM, activation to about 150% of control in presence of 1% Triton, inhibition to 20% of control without detergent
bilobalide
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20% activation at 0.01 mg/ml; an increase in GAD65 activity by 17.8% is observed with bilobalide; an increase in GAD65 activity by approximately 18% is observed with bilobalide
Br-
-
activates
CaCl2
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0.5 mM, pH 5.6, 45% increase in activity
Calmodulin
Cl-
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activates
CTP
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2 mM, activation to about 110% of control without detergent. Activation to about 200% of control in presence of 1% Triton X-100
EDTA
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2 mM, stimulates
F-
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activates
Glutarate
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stimulates
GTP
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2 mM, activation to about 125% of control without detergent. Activation to about 190% of control in presence of 1% Triton X-100
I-
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activates
L-Gln
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activates 18% at 1 mM
PCMB
-
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UTP
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2 mM, activation to about 140% of control without detergent. Activation to about 190% of control in presence of 1% Triton X-100
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.2
cysteine sulfinic acid
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1.04
L-alpha-Methylglutamate
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pH 4.6, 25°C
5.4
L-cysteic acid
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0.174 - 22
L-Glu
0.0274 - 32.3
L-glutamate
additional information
additional information
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