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Information on EC 4.1.1.15 - glutamate decarboxylase and Organism(s) Rattus norvegicus and UniProt Accession Q05683
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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: Rattus norvegicus
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
-
-
-
-
GAD67
GADCase
-
-
-
-
gamma-Glutamate decarboxylase
-
-
-
-
GDCase
-
-
-
-
Glutamic acid decarboxylase
glutamic acid decarboxylase 67
Glutamic decarboxylase
-
-
-
-
L-Aspartate-alpha-decarboxylase
-
-
-
-
L-Glutamate alpha-decarboxylase
-
-
-
-
L-Glutamate decarboxylase
-
-
-
-
L-Glutamic acid decarboxylase
L-Glutamic decarboxylase
-
-
-
-
MGAD
-
-
-
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GAD
-
-
-
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Glutamic acid decarboxylase
-
-
-
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glutamic acid decarboxylase 67
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67 kDa form of the 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-Asp
?
-
Phe or 6-azauracil decrease specificity for L-Glu and increase specificity to L-Asp
-
-
?
L-Glu
4-Aminobutanoate + CO2
-
6-azauracil or Phe decrease specificity for L-Glu and increased specificity to L-Asp
-
-
?
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
-
glutamate decarboxylase is the rate-limiting enzyme in the synthesis of gamma-aminobutyric acid, the most important inhibitory neurotransmitter in central nervous system
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
the enzyme activity is higher in hippocampus of old rats compared to young rats
-
-
?
additional information
?
-
-
calpains inhibit the GAD cleavage in vivo, overview
-
-
?
additional information
?
-
-
chronic systemic administration of an agonist of dopamine D1/D5-preferring receptors increases GAD mRNA levels in striatonigral neurons in intact and dopamine-depleted rats. striatal GAD67 mRNA levels were negatively correlated with nigral alpha1 mRNA levels in the dopamine-depleted but not dopamine-intact side. down-regulation of nigral GABAA receptors is linked to the increase in striatal GAD67 mRNA levels in the dopamine-depleted striatum. Different signaling pathways are involved in the modulation by dopamine D1/D5 receptors of GAD65 and GAD67 mRNA levels in striatonigral neurons, overview
-
-
?
additional information
?
-
-
GAD65 plays an essential role in neurotransmission, overview
-
-
?
additional information
?
-
-
regular performance of exercise results in extensive changes in the forebrain GABAergic system that may be implicated in the changes in stress sensitivity and emotionality observed in exercising subjects, overview
-
-
?
additional information
?
-
-
SDF1alpha/CXCR4/G protein/ERK signaling induces the expression of the GAD67 system via Egr1 activation, a mechanism that may promote the maturation of GABAergic neurons during development
-
-
?
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
-
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
-
glutamate decarboxylase is the rate-limiting enzyme in the synthesis of gamma-aminobutyric acid, the most important inhibitory neurotransmitter in central nervous system
-
-
?
L-glutamate
4-aminobutanoate + CO2
-
the enzyme activity is higher in hippocampus of old rats compared to young rats
-
-
?
additional information
?
-
-
calpains inhibit the GAD cleavage in vivo, overview
-
-
?
additional information
?
-
-
chronic systemic administration of an agonist of dopamine D1/D5-preferring receptors increases GAD mRNA levels in striatonigral neurons in intact and dopamine-depleted rats. striatal GAD67 mRNA levels were negatively correlated with nigral alpha1 mRNA levels in the dopamine-depleted but not dopamine-intact side. down-regulation of nigral GABAA receptors is linked to the increase in striatal GAD67 mRNA levels in the dopamine-depleted striatum. Different signaling pathways are involved in the modulation by dopamine D1/D5 receptors of GAD65 and GAD67 mRNA levels in striatonigral neurons, overview
-
-
?
additional information
?
-
-
GAD65 plays an essential role in neurotransmission, overview
-
-
?
additional information
?
-
-
regular performance of exercise results in extensive changes in the forebrain GABAergic system that may be implicated in the changes in stress sensitivity and emotionality observed in exercising subjects, overview
-
-
?
additional information
?
-
-
SDF1alpha/CXCR4/G protein/ERK signaling induces the expression of the GAD67 system via Egr1 activation, a mechanism that may promote the maturation of GABAergic neurons during development
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
bound cofactor. The enzyme is present in large amounts as apoenzyme, that can by activated when additional 4-aminobutanoate synthesis is required
pyridoxal 5'-phosphate
-
although GAD65 and GAD67 interact differently with pyridoxal 5'-phosphate, their cofactor-binding sites contain the same set of nine putative cofactor-binding residues and has the same basic structural fold. Thus the cofactor-binding differences cannot by attributed to fundamental structural differences between the GADs but must result from subtle modifications of the basic cofactor-binding fold
pyridoxal 5'-phosphate
-
slower binding of pyridoxal 5'-phosphate to GAD67 than to GAD65, and less ease to dissociate pyridoxal 5'-phosphate from holoGAD67 than holoGAD54. TGAD67 is more highly saturated by the cofactor than GAD65. The two binding sites of GAD65 exhibit similar affinities for pyridoxal 5'-phosphate. One binding site of GAD67 exhibits a significantly higher affinity for pyridoxal 5'-phosphate than the other binding site
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
in presence of leupeptin in freshly prepared homogenates. Inhibition of enzyme from homogenates stored without Triton X-100 for 24 h at 4°C
additional information
-
chronic mild stress leads to 60% reduced enzyme activity in old rats, which is reversible by neuronal nitric oxide synthase inhibitor 7-nitroindazole, overview
-
additional information
-
ionomycin inhibits the expression of the full-length enzyme, but not of the truncated mutant, while mu-calpain and calpastatin inhibit the truncated enzyme, but not the full-length wild-type enzyme in the synaptosome, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
2 mM, activation to about 170% of control without detergent. Activation to about 210% of control in presence of 1% Triton X-100
AMP
-
2 mM, activation to about 125% of control without detergent. Activation to about 140% of control in presence of 1% Triton X-100
ATP
-
2 mM, activation to about 150% of control in presence of 1% Triton, inhibition to 20% of control without detergent
CTP
-
2 mM, activation to about 110% of control without detergent. Activation to about 200% of control in presence of 1% Triton X-100
GTP
-
2 mM, activation to about 125% of control without detergent. Activation to about 190% of control in presence of 1% Triton X-100
UTP
-
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
isozyme GAD65 is activated by phosphorylation
-
additional information
-
6-azauracil and Phe decrease specificity for L-Glu and increased specificity to L-Asp
-
additional information
-
increased GAD or vGAT mRNA levels after acute SKF-81297 occurr in striatonigral neurons. Subchronic SKF-81297 induces significant increases in striatal GAD67, GAD65, preprodynorphin, and vGAT mRNA levels and decreases in nigral alpha1 mRNA levels. In the striatum contralateral to the 6-OHDA lesion, subchronic but not acute SKF-81297 induced a significant increase in GAD65 mRNA levels
-
additional information
-
stromal cell-derived factor alpha, SDF1alpha, rapidly induces the expression of the early growth response gene Egr1, a transcription factor involved in activity-dependent neuronal responses, in a concentration-dependent manner, which increases the expression of GAD67 at both the mRNA and protein levels, and increases the amount and neurite localization of gamma-aminobutyric acid, GABA, in neurons already expressing GABA. SDF1alpha-induced Egr1/GAD67 expression is mediated by the G protein-coupled CXCR4 receptor and activation of the ERK pathway, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.18
L-glutamate
-
isoform GAD67, treated with trypsin, which also increases vmax value by 31%
1.33
L-glutamate
-
isoform GAD65, treated with trypsin, which also increases vmax value by 33%
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme activity in hippocampi of young and old rats
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoform GAD65, mainly in middle and upper portions of villi, GAD65 is not found in goblet cells, and GAD67 is not detected in jejunum at all
additional information
-
-
-
glutamic acid decarboxylase in E18 embryonic hippocampal neurons
-
the enzyme activity is higher in hippocampus of old rats compared to young rats
-
the renal enzyme differs from the brain and pancreatic enzyme by its strong binding to membranes that is not influenced by detergents
-
the 58-kDa GAD65, N-terminal 69 amino acids truncated form of full-length GAD65 protein, is developmentally expressed during post-natal testis maturation
additional information
-
GAD65, GAD67, PPD and vGAT mRNA levels in the striatum and GABAA receptor alpha1 subunit mRNA levels in the substantia nigra, pars reticulata, and striatum in rats with single or subchroninc application of unilateral 6-hydroxydopamine lesion, overview
additional information
-
GAD67 tissue expression pattern in exercised and nonexercised rats, overview
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
-
more than 90% of GAD activity occurs in the cytosolic fraction. Isoform GAD67 is exclusively expressed in the cytosolic fraction
-
the renal enzyme differs from the brain and pancreatic enzyme by its strong binding to membranes that is not influenced by detergents
-
three distinct moieties of glutamate decarboxylase localize to membrane compartments, an amphiphilic GAD65 homodimer, an amphiphilic GAD65/67 heterodimer, tethered to membranes via the GAD65 subunit and a hydrophilic GAD67 homodimer, which associates with membranes by a distinct mechanism
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
isozyme GAD65 is activated by phosphorylation on Thr95. Protein kinase C isoform epsilon is the protein kinase responsible for phosphorylation and regulation of GAD65. Role of phosphorylation of GAD65 in regulation of GABA neurotransmission. Effect of neuronal stimulation on the level of membrane associated GAD (mGAD and GAD65) and soluble GAD (sGAD and GAD67), overview
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). DCE2_RAT
585
0
65402
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
58000
-
SDS-PAGE, N-terminal 69 amino acids truncated form of full-length GAD65 protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
dimer-forming interactions are mediated mainly by carboxyl-terminal domain
additional information
additional information
-
N-terminal segments of both GAD65 and GAD67 are exposed and flexible
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
phosphoprotein
isozyme GAD65 is activated by phosphorylation at T95, identification of potential phosphorylation sites S3, S6, T95, and S417 on rGAD65 by tandem MS/MS spectrometry. The effect of phosphorylation on GAD65 can be reversed by treatment with protein phosphatases. Protein kinase C isoform epsilon is the protein kinase responsible for phosphorylation and regulation of GAD65
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, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of a C-terminal 44-kDa truncated GAD, i.e. GAD44. GAD25 corresponds to the putative regulatory domain of the full-length protein, GAD44 contains the cofactor-binding site and enzymatic activity for synthesis of gamma-butyric acid
additional information
-
the recombinant human enzyme injected into LEW.1A rats shows a half-life of 2.77 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
preparation of native enzyme in rat brain synaptosomes, isolation of KCl-stimulated P2'-synaptosomes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of deletion mutant (rGAD65)C45A/DELTA1-38 and (rGAD65)DELTA1-101, expression in COS-7 cells
-
expression of the full-length and truncated mutant enzymes, expression analysis
-
gene GAD67, cloning of four GAD67 transcripts, GAD67-C1, -C2, -C3, and -C4, produced by alternative splicing and polyadenlyation and translating a GAD protein with truncated pyridoxal 5'-phosphate binding domain, which leads to a lack of glutamate decarboxylase activity, expression in HEK-293 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
exposure of cell cultures to intermittent hypoxia decreases GAD67 activity. intermittent hypoxia-evoked decrease in GAD67 activity is caused by increased cAMP - protein kinase A - dependent phosphorylation of GAD67, but not as a result of changes in either GAD67 mRNA or protein expression
-
GAD65 gene expression is dynamically regulated at multiple levels during post-natal testis maturation, GAD65 protein is presented in Leydig cells of day 1 testis, primary spermatocytes and spermatids of postnatal of day 90 testis
-
in the herpes simplex virus-GAD group, GAD67 mRNA and protein levels are significantly increased in the L6-S1 dorsal root ganglia
-
subchronic L-DOPA administration (6 mg/kg) is paralleled by a significant increase in mRNA levels of the two isoforms of glutamic acid decarboxylase (GAD67 and GAD65), 1 mg/kg 2-methyl-6-(phenylethynyl)-pyridine completely reverses the effects of L-DOPA on GAD67 and GAD65 and reduces the increases in mRNA levels
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
most important application of glutamate decarboxylase antibodies is to identify those neurons and neuronal projections that use 4-aminobutanoate as their neurotransmitter by immunocytochemical visualization
medicine
medicine
-
eight hours following kainate- or pilocarpine-induced seizure of piriform cortex, severe neuronal damage is observed accompanied by significant decreases in enzyme protein. In layer II of the central pirifiorm cortex, significant increase in isoforms GAD65 and GAD67 mRNA is determined
medicine
-
herpes simplex virus -based GAD gene transfer to bladder afferent pathways represents an approach for treatment of neurogenic detrusor overactivity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Denner, L.A.; Wei, S.C.; Lin, H.S.; Lin, C.T.; Wu, J.Y.
Brain L-glutamate decarboxylase: purification and subunit structure
Proc. Natl. Acad. Sci. USA
84
668-672
1987
Rattus norvegicus
Wu, J.Y.; Denner, L.; Lin, C.T.; Song, G.
L-Glutamate decarboxylase from brain
Methods Enzymol.
113
3-10
1985
Rattus norvegicus
Yamaguchi, T.; Matsumura, Y.
Purification of L-glutamate decarboxylase by affinity chromatography
Biochim. Biophys. Acta
481
706-711
1977
Rattus norvegicus
Tunnicliff, G.
Action of inhibitors on brain glutamate decarboxylase
Int. J. Biochem.
27
1235-1241
1990
Gallus gallus, Mus musculus, Rattus norvegicus, Sus scrofa
Martin, D.L.; Martin, S.B.; Wu, S.J.; Espina, N.
Regulatory properties of brain glutamate decarboxylase (GAD): the apoenzyme of GAD is present principally as the smaller of two molecular forms of GAD in brain
J. Neurosci.
11
2725-2731
1991
Rattus norvegicus
Chen, C.H.; Battaglioli, G.; Martin, D.L.; Hobart, S.A.; Colon, W.
Distinctive interactions in the holoenzyme formation for two isoforms of glutamate decarboxylase
Biochim. Biophys. Acta
1645
63-71
2003
Rattus norvegicus
Tursky, T.; Bandzuchova, E.
An endogenous activator of renal glutamic acid decarboxylase effects of adenosine triphosphate, phosphate and chloride on the activity of this enzyme
Eur. J. Biochem.
262
696-703
1999
Rattus norvegicus
Kanaani, J.; Lissin, D.; Kash, S.F.; Baekkeskov, S.
The hydrophilic isoform of glutamate decarboxylase, GAD67, is targeted to membranes and nerve terminals independent of dimerization with the hydrophobic membrane-anchored isoform, GAD65
J. Biol. Chem.
274
37200-37209
1999
Rattus norvegicus
Martin, D.L.; Liu, H.; Martin, S.B.; Wu, S.J.
Structural features and regulatory properties of the brain glutamate decarboxylases
Neurochem. Int.
37
111-119
2000
Rattus norvegicus
Battaglioli, G.; Liu, H.; Hauer, C.R.; Martin, D.L.
Glutamate decarboxylase: loss of N-terminal segment does not affect homodimerization and determination of the oxidation state of cysteine residues
Neurochem. Res.
30
989-1001
2005
Rattus norvegicus
Wang, F.Y.; Watanabe, M.; Zhu, R.M.; Maemura, K.
Characteristic expression of gamma-aminobutyric acid and glutamate decarboxylase in rat jejunum and its relation to differentiation of epithelial cells
World J. Gastroenterol.
10
3608-3611
2004
Rattus norvegicus
Freichel, C.; Potschka, H.; Ebert, U.; Brandt, C.; Loescher, W.
Acute changes in the neuronal expression of GABA and glutamate decarboxylase isoforms in the rat piriform cortex following status epilepticus
Neuroscience
141
2177-2194
2006
Rattus norvegicus
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
Luo, Y.; Lathia, J.; Mughal, M.; Mattson, M.P.
SDF1alpha/CXCR4 signaling, via ERKs and the transcription factor Egr1, induces expression of a 67-kDa form of glutamic acid decarboxylase in embryonic hippocampal neurons
J. Biol. Chem.
283
24789-24800
2008
Rattus norvegicus
Hill, L.E.; Droste, S.K.; Nutt, D.J.; Linthorst, A.C.; Reul, J.M.
Voluntary exercise alters GABAA receptor subunit and glutamic acid decarboxylase-67 gene expression in the rat forebrain
J. Psychopharmacol. (Oxford)
24
745-756
2010
Rattus norvegicus
Liu, H.; Wang, Z.; Li, S.; Zhang, Y.; Yan, Y.C.; Li, Y.P.
Utilization of an intron located polyadenlyation site resulted in four novel glutamate decarboxylase transcripts
Mol. Biol. Rep.
36
1469-1474
2008
Rattus norvegicus
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)
Yamamoto, N.; Soghomonian, J.
Time-course of SKF-81297-induced increase in glutamic acid decarboxylase 65 and 67 mRNA levels in striatonigral neurons and decrease in GABAA receptor alpha 1 subunit mRNA levels in the substantia nigra, pars reticulata, in adult rats with a unilateral 6-hydroxydopamine lesion
Neuroscience
154
1088-1099
2008
Rattus norvegicus
El-Faramawy, Y.A.; El-Banouby, M.H.; Sergeev, P.; Mortagy, A.K.; Amer, M.S.; Abdel-Tawab, A.M.
Changes in glutamate decarboxylase enzyme activity and tau-protein phosphorylation in the hippocampus of old rats exposed to chronic mild stress: Reversal with the neuronal nitric oxide synthase inhibitor 7-nitroindazole
Pharmacol. Biochem. Behav.
91
339-344
2009
Rattus norvegicus
Liu, H.; Li, S.; Zhang, Y.; Yan, Y.; Li, Y.
Dynamic regulation of glutamic acid decarboxylase 65 gene expression in rat testis
Acta Biochim. Biophys. Sin.
41
545-553
2009
Rattus norvegicus
Miyazato, M.; Sugaya, K.; Goins, W.F.; Wolfe, D.; Goss, J.R.; Chancellor, M.B.; de Groat, W.C.; Glorioso, J.C.; Yoshimura, N.
Herpes simplex virus vector-mediated gene delivery of glutamic acid decarboxylase reduces detrusor overactivity in spinal cord-injured rats
Gene Ther.
16
660-668
2009
Rattus norvegicus
Yamamoto, N.; Soghomonian, J.J.
Metabotropic glutamate mGluR5 receptor blockade opposes abnormal involuntary movements and the increases in glutamic acid decarboxylase mRNA levels induced by l-DOPA in striatal neurons of 6-hydroxydopamine-lesioned rats
Neuroscience
163
1171-1180
2009
Rattus norvegicus
Raghuraman, G.; Prabhakar, N.R.; Kumar, G.K.
Post-translational modification of glutamic acid decarboxylase 67 by intermittent hypoxia: evidence for the involvement of dopamine D1 receptor signaling
J. Neurochem.
115
1568-1578
2010
Rattus norvegicus
Chou, C.C.; Modi, J.P.; Wang, C.Y.; Hsu, P.C.; Lee, Y.H.; Huang, K.F.; Wang, A.H.; Nan, C.; Huang, X.; Prentice, H.; Wei, J.; Wu, J.Y.
Activation of brain L-glutamate decarboxylase 65 isoform (GAD65) by phosphorylation at threonine 95 (T95)
Mol. Neurobiol.
54
866-873
2017
Homo sapiens (Q05329), Homo sapiens (Q99259), Homo sapiens, Rattus norvegicus (Q05683), Rattus norvegicus Sprague Dawley (Q05683)
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