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Information on EC 4.1.1.15 - glutamate decarboxylase and Organism(s) Mus musculus and UniProt Accession P48318
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4.1.1.15 glutamate decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.
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Word Map
- 4.1.1.15
-
gabaergic
-
gamma-aminobutyric
- autoimmune
- autoantibody
- islet
- mellitus
-
neurotransmitter
- synaptic
- hippocampus
-
interneurons
- cortical
- autoantigens
- choline
-
excitatory
-
dorsal
- striatum
-
insulin-dependent
-
ventral
- seizure
- parvalbumin
- epilepsy
- beta-cell
-
cholinergic
-
glutamatergic
- synapses
-
medial
-
neurotransmission
-
neurochemical
-
substantia
-
afferent
-
postsynaptic
- c-peptide
-
somata
-
chat
-
presynaptic
-
antibody-positive
-
autoreactive
- ketoacidosis
- bicuculline
- gaba-transaminase
- colliculus
-
preoptic
- gaba-t
-
calretinin
-
rostral
- muscimol
-
boutons
- reelin
- calbindin
- analysis
- synthesis
- pharmacology
- nutrition
- medicine
- food industry
- diagnostics
-
glycinergic
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glutamic acid decarboxylase, gad65, gad67, glutamate decarboxylase, glutamic acid decarboxylase 65, glutamic acid decarboxylase 67, gad-65, gad-67, glutamate decarboxylase 67, l-glutamate decarboxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
65 kDa glutamic acid decarboxylase
-
-
-
-
67 kDa glutamic acid decarboxylase
-
-
-
-
Aspartate 1-decarboxylase
-
-
-
-
Aspartic alpha-decarboxylase
-
-
-
-
Cysteic acid decarboxylase
-
-
-
-
Decarboxylase, glutamate
-
-
-
-
ERT D1
-
-
-
-
GAD
GAD-65
-
-
-
-
GAD-67
-
-
-
-
GAD-alpha
-
-
-
-
GAD-beta
-
-
-
-
GAD-gamma
-
-
-
-
GAD65
GADCase
-
-
-
-
gamma-Glutamate decarboxylase
-
-
-
-
GDCase
-
-
-
-
Glutamic acid decarboxylase
Glutamic decarboxylase
-
-
-
-
L-Aspartate-alpha-decarboxylase
-
-
-
-
L-Glutamate alpha-decarboxylase
-
-
-
-
L-Glutamate decarboxylase
-
-
-
-
L-Glutamic acid decarboxylase
L-Glutamic decarboxylase
-
-
-
-
MGAD
-
-
-
-
GAD
-
-
-
-
Glutamic acid decarboxylase
-
-
-
-
L-Glutamic acid decarboxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
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
9024-58-2
-
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
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme in controlling GABA synthesis, GABA is synthesized by GAD67 is used for the other functions such as trophic factor for neuronal development or energy source. GAD67 is constitutively active and is responsible for the basal GABA production while GAD65 is transiently activated in response to the extra demand of GABA in neurotransmission
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme in neurotransmitter gamma-aminobutyric acid, GABA, biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD65-mediated GABA synthesis is critical for the consolidation of stimulus-specific fear memory. This function appears to involve a modulation of neural activity patterns in the amygdalo-hippocampal pathway as indicated by a reduction in theta frequency synchronization between the amygdala and hippocampus of Gad65-/- mice during the expression of generalized fear memory
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD67 is the rate-limiting enzyme of GABA biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
nicotine, by activating nAChRs located on cortical or hippocampal GABAergic interneurons, can up-regulate GAD67 expression via an epigenetic mechanism
-
-
?
additional information
?
-
-
isoform GAD65 plays a major role in gamma-aminobutanoate transmission in normal physiological condition. Isoform GAD67 can serve this role under some pathological conditions
-
-
?
additional information
?
-
-
cortical GABAergic neurons, surviving pathological insult such as ischemia or brain trauma, exposed to glutamate in vitro, display an NMDA receptor-mediated alteration in the levels of the GABA synthesizing enzyme glutamic acid decarboxylase, isozymes GAD65 and 67, mechanism of glutamate excitotoxicity, overview
-
-
?
additional information
?
-
-
GAD65 plays an essential role in neurotransmission, overview
-
-
?
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
L-glutamate
4-aminobutanoate + CO2
-
-
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme in controlling GABA synthesis, GABA is synthesized by GAD67 is used for the other functions such as trophic factor for neuronal development or energy source. GAD67 is constitutively active and is responsible for the basal GABA production while GAD65 is transiently activated in response to the extra demand of GABA in neurotransmission
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD is the rate-limiting enzyme in neurotransmitter gamma-aminobutyric acid, GABA, biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD65-mediated GABA synthesis is critical for the consolidation of stimulus-specific fear memory. This function appears to involve a modulation of neural activity patterns in the amygdalo-hippocampal pathway as indicated by a reduction in theta frequency synchronization between the amygdala and hippocampus of Gad65-/- mice during the expression of generalized fear memory
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
GAD67 is the rate-limiting enzyme of GABA biosynthesis
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
nicotine, by activating nAChRs located on cortical or hippocampal GABAergic interneurons, can up-regulate GAD67 expression via an epigenetic mechanism
-
-
?
additional information
?
-
-
isoform GAD65 plays a major role in gamma-aminobutanoate transmission in normal physiological condition. Isoform GAD67 can serve this role under some pathological conditions
-
-
?
additional information
?
-
-
cortical GABAergic neurons, surviving pathological insult such as ischemia or brain trauma, exposed to glutamate in vitro, display an NMDA receptor-mediated alteration in the levels of the GABA synthesizing enzyme glutamic acid decarboxylase, isozymes GAD65 and 67, mechanism of glutamate excitotoxicity, overview
-
-
?
additional information
?
-
-
GAD65 plays an essential role in neurotransmission, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
removing extracellular calcium prevents the NMDAR-mediated decrease in GAD protein levels, whereas inhibiting calcium entry through voltage-gated calcium channels has no effect
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
-
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
-
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-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
-
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
-
4,4'-(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-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-[(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
-
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
-
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
-
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
-
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
-
1-Methylimidazole
-
about 85% residual activity at 5 mM, about 77% residual activity at 10 mM, about 65% residual activity at 20 mM
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-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
-
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
-
4,4'-(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-methylimidazole
-
about 75% residual activity at 5 mM, about 70% residual activity at 10 mM, about 58% residual activity at 20 mM
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-[(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
-
isoniazide
isoniazide-induced seizures are mediated primarily through competition with the cofactor pyridoxal 5'-phosphate resulting in the inhibition of GAD activity
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
-
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
-
additional information
-
downregulation of reelin and GAD67 expression by the increase of DNA-methyltransferase 1-mediated hypermethylation of promoters in GABAergic interneurons of the telencephalon
-
additional information
-
glutamate reduces the expression of isozymes GAD65 and GAD67, glutamate's suppressing effect on GAD protein isoforms is significantly attenuated by preincubation with the cysteine protease inhibitor N-acetyl-L-leucyl-L-leucyl-L-norleucinal via blockade of calpain and cathepsin protease activities, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
nicotine decreases inhibitory DNA-methyltransferase 1 mRNA and protein and increases GAD67 expression in the mouse frontal cortex, it diminishes the level of cytosine-5-methylation in the GAD67 promoter and prevents the methionine-induced hypermethylation of the same promoter. Nicotine effects are prevented by pretreatment with mecamylamine, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0266
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0418
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.012
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0142
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0047
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0209
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0052
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0108
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0127
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0126
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0002
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0079
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0072
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.013
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0045
4-(morpholin-4-yl)naphthalene-1,2-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0047
4-(piperidin-1-yl)naphthalene-1,2-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.065
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0112
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0083
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0104
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0129
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0593
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0057
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0049
biphenyl-3,3'-dicarbaldehyde
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.002 - 4
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0125
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0164
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0022
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0044
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0591
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
[(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)oxy]acetic acid
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0123
(4Z,7E)-N,N'-dihydroxy-2,2-dimethyl-5,6-dihydro-2H-benzimidazole-4,7-diimine
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0033
(5Z)-2-amino-5-(2-nitrobenzylidene)-1,3-thiazol-4(5H)-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.004
1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl 2,3,4-tri-O-acetylpentopyranoside
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0069
1-(2-nitrobenzyl)-1H-indole-3-carbaldehyde
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.002
10H-indeno[2,1-e]tetrazolo[1,5-b][1,2,4]triazin-10-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0777
2,4-bis[2-(4-hydroxyphenyl)propan-2-yl]phenol
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0073
2-(benzylsulfanyl)-3-(morpholin-4-yl)-2,3-dihydronaphthalene-1,4-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0087
2-chloro-N-[5-([2-oxo-2-[(4-sulfamoylphenyl)amino]ethyl]sulfanyl)-1,3,4-thiadiazol-2-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0042
2-hydroxy-2-(2-hydroxy-6-oxocyclohex-2-en-1-yl)-1H-indene-1,3(2H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.01
2-thioxo-3-[(E)-(3,3,5-trimethylcyclohexylidene)amino]-1,3-thiazolidin-4-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0845
2-[(2-chloro-5-nitrobenzoyl)amino]-5-iodobenzoic acid
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0089
2-[(3-formyl-1H-indol-1-yl)methyl]benzonitrile
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0004
3,3'-(4H-1,2,4-triazole-3,5-diyl)bis(4-nitro-1,2,5-oxadiazole)
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
3-[(2E)-2-[1-(3,4-dimethoxyphenyl)ethylidene]hydrazinyl]benzoic acid
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0064
3-[(E)-(2,6-difluorobenzylidene)amino]-2-thioxo-1,3-thiazolidin-4-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.012
4,4'-(phenylmethanediyl)bis[2-(4-chlorophenyl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one]
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0138
4,4'-[(4-hydroxyphenyl)methanediyl]bis(2-heptyl-5-methyl-2,4-dihydro-3H-pyrazol-3-one)
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0029
4-(morpholin-4-yl)naphthalene-1,2-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.003
4-(piperidin-1-yl)naphthalene-1,2-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0077
4-nitro-1,6-dihydrobenzo[1,2-d:3,4-d']bis[1,2,3]triazole
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.1
4-nitro-7-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]-2,1,3-benzothiadiazole
Mus musculus
above, pH 8.0, 37°C, recombinant enzyme
0.0064
4-[(1,4-dioxo-1,2,3,4-tetrahydronaphthalen-2-yl)sulfanyl]butanoic acid
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0033
5,6-dichloro-2,1,3-benzothiadiazole-4,7-diol
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0069
5-[(E)-benzylideneamino]-6-[(2-hydroxyethyl)amino]pyrimidine-2,4(1H,3H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0065
5-[(E)-[[1-(2-chlorobenzyl)-1H-indol-3-yl]methylidene]amino]-1,3-dihydro-2H-benzimidazol-2-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0558
5-[[5-hydroxy-3-methyl-1-(4-methylphenyl)-1H-pyrazol-4-yl]methylidene]-1,3-diphenyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0023
6,11-dioxo-5a,6,11,11a-tetrahydronaphtho[2',3':4,5][1,3]thiazolo[3,2-a]pyridin-12-ium
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0143
9H-indeno[1,2-b][1,2,5]oxadiazolo[3,4-e]pyrazin-9-one
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0049
biphenyl-3,3'-dicarbaldehyde
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.001
methyl 2-amino-3-oxo-3H-phenothiazine-1-carboxylate
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0065
methyl 2-[[(2-methylimidazo[1,2-a]pyridin-3-yl)carbonyl]amino]benzoate
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0076
N-(2-hydroxy-1,3-dioxo-2,3-dihydro-1H-inden-2-yl)benzamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0012
N-[4,7-dioxo-6-(phenylamino)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0022
N-[4,7-dioxo-6-(piperidin-1-yl)-4,7-dihydro-2,1,3-benzoxadiazol-5-yl]acetamide
Mus musculus
pH 8.0, 37°C, recombinant enzyme
0.0041
naphtho[2',3':4,5]imidazo[1,2-a]pyridine-6,11-dione
Mus musculus
pH 8.0, 37°C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.5
-
pH 6.0: about 80% of maximal activity, pH 7.5: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
-
GABAergic neurons, non-pyramidal cells of types A-C, and principal cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
palmitoylated GAD65 co-localizes with Rab5 in Golgi membranes and axons, and Rab5 regulates the trafficking of palmitoylated GAD65 from Golgi membranes to axons in an endosomal trafficking pathway
-
palmitoylated GAD65 co-localizes with Rab5 in Golgi membranes and axons, and Rab5 regulates the trafficking of palmitoylated GAD65 from Golgi membranes to axons in an endosomal trafficking pathway
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
-
GAD65-mediated 4-aminobutanoate synthesis plays relatively small but significant roles in nociceptive processing via supraspinal mechanisms
malfunction
-
GAD65 knockout mice show a diminished response to propofol, but not ketamine, indicating that GAD65-mediated 4-aminobutanoate synthesis plays an important role in hypnotic and immobilizing actions of propofol
malfunction
-
the GAD65 null mutation affects neural activities during fear memory extinction and examined local field potentials from the lateral amygdala, the CA1 area of the hippocampus, and the infralimbic area of the prefrontal cortex during this process in Gad65deficient mice
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). DCE1_MOUSE
593
0
66648
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
-
2 * 44000, high speed equilibrium sedimentation after treatment with 6 M guanidine HCl and 0.1 M beta-mercaptoethanol
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 44000, high speed equilibrium sedimentation after treatment with 6 M guanidine HCl and 0.1 M beta-mercaptoethanol
additional information
-
25 and 44 kDa GAD through differential GAD67 RNA splicing, the 25 kDa is enzymatically inactive and is present usually early in the development, the 44 kDa GAD is enzymatically active
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
palmitoylation of cysteines 30 and 45 is critical for post-Golgi trafficking of GAD65 to presynaptic sites and for its relative dendritic exclusion, leading to the presynaptic clustering of GAD65
phosphoprotein
-
protein kinase A is responsible for phosphorylation and inhibition of GAD67 activity, while calcineurin is the phosphatase responsible for dephosphorylation and activation of GAD67
proteolytic modification
proteolytic modification
-
conversion of full-length GAD65 to truncated GAD65 is not the result of random post-mortem degradation, but that it is an intracellular process that is highly regulated. The cleavage is mediated by calpain, a Ca2+-dependent cysteine protease
proteolytic modification
-
the purified recombinant GAD67 is cleaved by mu-calpain at specific sites in Ca2+-dependent manner. In brain synaptosomal preparation, GAD67 is cleaved to its truncated form by an endogenous protease which is inhibited by specific calpain inhibitors. In mu-calpain knockout mice, the level of tGAD in the brain is greatly reduced compared with the wild type. When mu-calpain gene is silenced by siRNA, the level of tGAD is also markedly reduced compared to the control group. Mu-calpain is activated by neuronal stimulation and Ca2+-influx. Calpastatin inhibits GAD67 processing, calpains inhibit the GAD cleavage in vivo, mutational analysis, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
isoform GAD65 knock-out mice show upregulated level of vesicular gamma-aminobutanoate transporter, and no change in the synaptic vesicles-associated isoform GAD67. In mutant mice, synaptic vesicles transport cytosolic gamma-aminobutanoate much more efficiently than wild-type
additional information
-
construction of cells overexpressing the GFP-tagged enzyme in membranes of cell somata, dendrites, axons and synaptic terminals of dentate neurons, subcellular localization, correlation to the amount of voltage-gated potassium channels Kv3.1b and Kv3.3, overview
additional information
-
construction of cerebellum-selective GAD67-knockout mice, selective GAD67 deletion in the cerebellum iss achieved using a Cre-loxP strategy. GABA level is reduced to 16-44% in the cerebellum but not in the cerebrum, inhibitory synaptic transmission to Purkinje cells is seriously impaired, however, the morphology of Purkinje cells and the density of synaptic terminals in the cerebellar cortex appears unaffected, phenotype, overview
additional information
-
construction of GFP-tagged GAD67 overexpressing mutant mice
additional information
-
targeted ablation of the GAD65 gene in Gad65-/- mice results in a pronounced context-independent, intramodal generalization of auditory fear memory during long-term/24 h or 14 d but not short-term/30 min memory retrieval, phenotype analysis, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gad67, expression of the isozyme as maltose-bindig protein fusion protein in Escherichia coli strain TB1
expression of the full-length and truncated mutant enzymes, expression analysis
-
GAD67 gene fragments from a TT2 cell genomic library, overexpression of the coding sequence of the EGFP-poly(A) gene in TT2 ES cells
-
gene gad65, expression of the enzyme as maltose-bindig protein fusion protein in Escherichia coli strain TB1
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
glutamic acid specific T-cells play a key role in type I diabetes. Isolation of several populations of glutamic acid decarboxylase peptide-specific T-cells from diabetes-prone non-obese and diabetes-resistant mice. The repertoire of T cells specific for these peptides is biased toward Tr cells that inhibit diabetes rather than toward pathogenic T cells that induce diabetes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wu, J.Y.; Matsuda, T.; Roberts, E.
Purification and characterization of glutamate decarboxylase from mouse brain
J. Biol. Chem.
248
3029-3034
1973
Mus musculus
Roberts, E.; Frankel, S.
Further studies of glutamic acid decarboxylase in brain
J. Biol. Chem.
190
505-512
1951
Mus musculus
Youngs, T.L.; Tunnicliff, G.
Substrate analogues and divalent cations as inhibitors of glutamate decarboxylase from Escherichia coli
Biochem. Int.
23
915-922
1991
Escherichia coli, Mus musculus
Tunnicliff, G.
Action of inhibitors on brain glutamate decarboxylase
Int. J. Biochem.
27
1235-1241
1990
Gallus gallus, Mus musculus, Rattus norvegicus, Sus scrofa
Liu, C.P.
Glutamic acid decarboxylase-specific CD4+ regulatory T cells
Ann. N. Y. Acad. Sci.
1079
161-170
2006
Mus musculus
Wu, H.; Jin, Y.; Buddhala, C.; Osterhaus, G.; Cohen, E.; Jin, H.; Wei, J.; Davis, K.; Obata, K.; Wu, J.Y.
Role of glutamate decarboxylase (GAD) isoform, GAD65, in GABA synthesis and transport into synaptic vesicles - Evidence from GAD65-knockout mice studies
Brain Res.
1154
80-83
2007
Mus musculus
Obata, K.; Hirono, M.; Kume, N.; Kawaguchi, Y.; Itohara, S.; Yanagawa, Y.
GABA and synaptic inhibition of mouse cerebellum lacking glutamate decarboxylase 67
Biochem. Biophys. Res. Commun.
370
429-433
2008
Mus musculus
Sha, D.; Jin, Y.; Wu, H.; Wei, J.; Lin, C.H.; Lee, Y.H.; Buddhala, C.; Kuchay, S.; Chishti, A.H.; Wu, J.Y.
Role of mu-calpain in proteolytic cleavage of brain L-glutamic acid decarboxylase
Brain Res.
1207
9-18
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Schlosser, M.; Walschus, U.; Kloeting, I.; Walther, R.
Determination of glutamic acid decarboxylase (GAD65) in pancreatic islets and its in vitro and in vivo degradation kinetics in serum using a highly sensitive enzyme immunoassay
Dis. Markers
24
191-198
2008
Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa, Rattus norvegicus LEW-1A
Monnerie, H.; Le Roux, P.D.
Glutamate alteration of glutamic acid decarboxylase (GAD) in GABAergic neurons: the role of cysteine proteases
Exp. Neurol.
213
145-153
2008
Mus musculus, Mus musculus BALB/c
Bergado-Acosta, J.R.; Sangha, S.; Narayanan, R.T.; Obata, K.; Pape, H.C.; Stork, O.
Critical role of the 65-kDa isoform of glutamic acid decarboxylase in consolidation and generalization of Pavlovian fear memory
Learn. Mem.
15
163-171
2008
Mus musculus
Wei, J.; Wu, J.Y.
Post-translational regulation of L-glutamic acid decarboxylase in the brain
Neurochem. Res.
33
1459-1465
2008
Mus musculus, Rattus norvegicus, Homo sapiens (Q05329), Homo sapiens (Q99259)
Alonso-Espinaco, V.; Elezgarai, I.; Diez-Garcia, J.; Puente, N.; Knoepfel, T.; Grandes, P.
Subcellular localization of the voltage-gated potassium channels Kv3.1b and Kv3.3 in the cerebellar dentate nucleus of glutamic acid decarboxylase 67-green fluorescent protein transgenic mice
Neuroscience
155
1059-1069
2008
Mus musculus, Mus musculus C57BL/6
El Idrissi, A.; L'Amoreaux, W.J.
Selective resistance of taurine-fed mice to isoniazide-potentiated seizures: In vivo functional test for the activity of glutamic acid decarboxylase
Neuroscience
156
693-699
2008
Mus musculus (P48320)
Kaneko, K.; Tamamaki, N.; Owada, H.; Kakizaki, T.; Kume, N.; Totsuka, M.; Yamamoto, T.; Yawo, H.; Yagi, T.; Obata, K.; Yanagawa, Y.
Noradrenergic excitation of a subpopulation of GABAergic cells in the basolateral amygdala via both activation of nonselective cationic conductance and suppression of resting K+ conductance: A study using glutamate decarboxylase 67-green fluorescent prote
Neuroscience
157
781-797
2008
Mus musculus
Satta, R.; Maloku, E.; Zhubi, A.; Pibiri, F.; Hajos, M.; Costa, E.; Guidotti, A.
Nicotine decreases DNA methyltransferase 1 expression and glutamic acid decarboxylase 67 promoter methylation in GABAergic interneurons
Proc. Natl. Acad. Sci. USA
105
16356-16361
2008
Homo sapiens, Mus musculus
Sangha, S.; Narayanan, R.T.; Bergado-Acosta, J.R.; Stork, O.; Seidenbecher, T.; Pape, H.C.
Deficiency of the 65 kDa isoform of glutamic acid decarboxylase impairs extinction of cued but not contextual fear memory
J. Neurosci.
29
15713-15720
2009
Mus musculus
Kubo, K.; Nishikawa, K.; Hardy-Yamada, M.; Ishizeki, J.; Yanagawa, Y.; Saito, S.
Altered responses to propofol, but not ketamine, in mice deficient in the 65-kilodalton isoform of glutamate decarboxylase
J. Pharmacol. Exp. Ther.
329
592-599
2009
Mus musculus
Kubo, K.; Nishikawa, K.; Ishizeki, J.; Hardy-Yamada, M.; Yanagawa, Y.; Saito, S.
Thermal hyperalgesia via supraspinal mechanisms in mice lacking glutamate decarboxylase 65
J. Pharmacol. Exp. Ther.
331
162-169
2009
Mus musculus
Sivertsen, T.; Nygaard, A.K.; Mathisen, G.; Fonnum, F.
Effects of 4-methylimidazole on cerebral glutamate decarboxylase activity and specific GABA receptor binding in mice
Toxicol. Mech. Methods
19
214-218
2009
Mus musculus, Mus musculus B6D2
Ilg, T.; Berger, M.; Noack, S.; Rohwer, A.; Gassel, M.
Glutamate decarboxylase of the parasitic arthropods Ctenocephalides felis and Rhipicephalus microplus: gene identification, cloning, expression, assay development, identification of inhibitors by high throughput screening and comparison with the orthologs
Insect Biochem. Mol. Biol.
43
162-177
2013
Ctenocephalides felis (K7WYY0), Ctenocephalides felis, Rhipicephalus microplus (K7XPX5), Rhipicephalus microplus, Drosophila melanogaster (P20228), Drosophila melanogaster, Mus musculus (P48318), Mus musculus (P48320), Mus musculus
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