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Information on EC 4.1.1.15 - glutamate decarboxylase and Organism(s) Homo sapiens and UniProt Accession Q05329

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.15 glutamate decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.
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This record set is specific for:
Homo sapiens
UNIPROT: Q05329
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The taxonomic range for the selected organisms is: Homo sapiens
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glutamic acid decarboxylase
-
glutamic acid decarboxylase 65
-
L-glutamate decarboxylase 65
-
L-Glutamic acid decarboxylase
-
65 kDa glutamic acid decarboxylase
-
-
-
-
67 kDa glutamic acid decarboxylase
-
-
-
-
Aspartate 1-decarboxylase
-
-
-
-
Aspartic alpha-decarboxylase
-
-
-
-
Cysteic acid decarboxylase
-
-
-
-
Decarboxylase, glutamate
-
-
-
-
ERT D1
-
-
-
-
GAD-65
-
-
-
-
GAD-67
-
-
-
-
GAD-alpha
-
-
-
-
GAD-beta
-
-
-
-
GAD-gamma
-
-
-
-
GAD2
-
-
GAD65
GAD67
GADCase
-
-
-
-
gamma-Glutamate decarboxylase
-
-
-
-
GDCase
-
-
-
-
glutamate decarboxylase
-
-
glutamate decarboxylase 1
-
-
glutamate decarboxylase 65
-
-
Glutamic acid decarboxylase
glutamic acid decarboxylase 65
glutamic acid decarboxylase-65
-
-
glutamic acid decarboxylase67
-
Glutamic decarboxylase
-
-
-
-
L-Aspartate-alpha-decarboxylase
-
-
-
-
L-Glutamate alpha-decarboxylase
-
-
-
-
L-Glutamate decarboxylase
-
-
-
-
L-glutamate decarboxylase 67
-
L-Glutamic acid decarboxylase
L-Glutamic decarboxylase
-
-
-
-
MGAD
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamate = 4-aminobutanoate + CO2
show the reaction diagram
reaction proceeds via radical mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate
4-aminobutanoate + CO2
show the reaction diagram
L-Glu
4-Aminobutanoate + CO2
show the reaction diagram
L-glutamate
4-aminobutanoate + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamate
4-aminobutanoate + CO2
show the reaction diagram
L-Glu
4-Aminobutanoate + CO2
show the reaction diagram
-
rate-limiting enzyme involved in the synthesis of gamma-aminobutyric acid
-
-
?
L-glutamate
4-aminobutanoate + CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Mercaptopropionic acid
-
allylglycine
-
betulinic acid
-
ursolic acid
-
valerenic acid
-
(E)-pent-2-enoic acid
-
20% inhibition at 0.01 mg/ml
2-oxoglutarate
-
-
3,4-dihydroxyphenylacetic acid
-
-
3-Hydroxytyramine
-
-
3-Mercaptopropionic acid
4'-deoxypyridoxine-5'-phosphate
-
about 60% inhibition of GAD65 at 3.5 mM, GAD67 is hardly affected
4'-O-methylpyridoxine-5'-phosphate
-
decreases activity of GAD65 in unphysiologically high concentrations, about 60% inhibition at 3.5 mM. GAD67 activity is hardly affected
allylglycine
-
-
asiaticoside
-
-
Asp
-
-
betulinic acid
-
27% inhibition at 0.01 mg/ml
bilobalide
-
-
D-Glu
-
-
DL-alpha-Aminoadipic acid
-
-
DL-Penicillamine
-
-
ginsenosides
-
23% inhibition at 0.01 mg/ml, ethanol extract of Panax quinquefolius, different glycoside derivatives, overview
-
L-Cysteine hydrochloride
-
-
L-cysteine sulfinic acid
-
-
ursolic acid
valerenic acid
-
20% inhibition at 0.01 mg/ml
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
asiaticoside
stimulates at 0.0104 mM in vitro by 22%. No stimulation is observed in the absence of pyridoxal 5'-phosphate, so it is unlikely that asiaticoside acts as a PLP mimic
bilobalide
stimulates at 0.0306 mM in vitro by 18%
apocalmodulin
-
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
-
asiaticoside
bilobalide
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.28 - 2.9
L-Glu
0.5 - 0.71
L-glutamate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41 - 7.7
L-Glu
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
NO
0.29 - 0.46
O2
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0123
3-Mercaptopropionic acid
Homo sapiens
recombinant MBP-tagged enzyme, pH 8.0, 37°C
0.0123
3-Mercaptopropionic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00024
recombinant GST-tagged enzyme, pH 8.0, 37°C
0.00038
recombinant MBP-tagged enzyme, pH 8.0, 37°C
0.039
-
mutant with N-terminal deletion of 70 amino acids, pH 7.2
0.041
-
mutant with N-terminal deletion of 90 amino acids, pH 7.2
0.216
-
wild-type, pH 7.2
1.37
-
-
1.85
-
GAD67
1.96
-
GAD65
2.956
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 8
assay at
6.8
-
-
7 - 7.5
-
broad
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.8
-
pH 6.0: about 65% of maximal activity, pH 7.8: about 35% of maximal activity
6.4 - 7.8
-
pH 6.4: about 50% of maximal activity, pH 7.8: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
37 - 42
-
GAD65-GST fusion protein expressed in Escherichia coli
39 - 43
43 - 50
45 - 50
-
GAD67 after cleavage with protease factor Xa
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
anterior cingulate cortex and superior temporal brain cortex
Manually annotated by BRENDA team
-
cerebrospinal fluid elicits physiopathological effects on cerebellar GABA synapses in vitro, cerebrospinal fluid IgG-induced depressive effects are abolished by absorption of GAD-antibodies using recombinant GAD. Furthermore, forskolin, an activator of cAMP, recovers the cerebrospinal fluid IgG-induced reduction of GABA release
Manually annotated by BRENDA team
-
mononuclear leukocyte, isoform GAD65 is expressed with its C-terminal end truncated
Manually annotated by BRENDA team
-
two isoforms ofGAD, GAD67and GAD65
Manually annotated by BRENDA team
-
isozyme GAD65
Manually annotated by BRENDA team
-
orbitofrontal, anterior cingulate, and dorsolateral
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
-
targeting of the processed enzyme
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
physiological function
isozyme GAD67 is inhibited by phosphorylation. Protein kinase A is the protein kinase responsible for phosphorylation and regulation of GAD67. 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?
DCE2_HUMAN
585
0
65411
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
gel filtration
140000
-
nondenaturing PAGE
65000
-
SDS-PAGE
67000
-
2 * 67000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 65000, SDS-PAGE
dimer
-
2 * 67000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
isozyme GAD65 is activated by phosphorylation at Thr95, while isozyme GAD67 is inhibited by phosphorylation. Gad65 is also phosphorylated at Ser417. The effect of phosphorylation on GAD65 and GAD67 can be reversed by treatment with protein phosphatases. Protein kinase A (PKA) and protein kinase C isoform epsilon are the protein kinases responsible for phosphorylation and regulation of GAD67 and GAD65, respectively
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
phosphoprotein
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
additional information
-
the enzyme undergoes posttranslational processing
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminally truncated mutants of both isoform GAD65 and GAD67. GAD67 shows a thethered loop covering the active site, providing a catalytic environment that sustains 4-aminobutanoate production. In isoform GAD65, the same catalytic loop is inherently mobile promoting a side reaction that results in cofactor release and enzyme autoinactivation
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C30A
mutation of Cys30 to Ala abolishes the presynaptic clustering of GAD65 in primary hippocampal neurons
C45A
mutation of Cys30 to Ala abolishes the presynaptic clustering of GAD65 in primary hippocampal neurons
T95A
site-directed mutagenesis, the mutation T95A of the phosphorylation site abolishes the phosphorylation and its effects on enzyme activity
T95E
site-directed mutagenesis, when the phosphorylation site T95 is mutated to glutamic acid, which mimics the phosphorylation status of hGAD65, the enzyme activity is greatly increased. An increase of GAD65 activity by 55% compared to the wild type hGAD65 is observed indicating that mutation of T95 to glutamic acid mimics the effect of phosphorylation
T91A
-
abolishes phosphorylation by protein kinase A and subsequent inhibition of enzyme activity
T91D
-
mimics the inhibiting effect of enzyme phosphorylation
T91E
-
mimics the inhibiting effect of enzyme phosphorylation
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
half-life of the recombinant enzyme is 1.27-2.35 h, unaffected by autoantibodies against the enzyme
50
-
50% loss of activity after 24 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stability is optimal over 3 months, in lyophilized form at 20°C
-
the recombinant human enzyme injected into LEW.1A rats shows a half-life of 2.77 h
-
using RNA polymerase sigma factor (RpoS) or glutathione transferase as fusion expression partners, the solubility of the enzyme significantly increases.
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme concentration of at least 3 mg/ml, under argon, in 100 mM potassium phosphate buffer containing 2 mM 2-aminoethylisothiouronium bromide and 0.4 mM pyridoxal 5'-phosphate
-
-80°C, 3 months. rGAD67/65 is stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged enzyme from Escherichia coli strain DH5alpha by glutathione affinity chromatography, recombinant MBP-tagged enzyme from Escherichia coli strain DH5alpha by amylose affinity chromatography
recombinant GST-tagged wild-type isozyme GAD65 from Escherichia coli strain DH5alpha by glutathione affinity chromatography and cleavage of the GST-tag by Factor Xa, followed by another step of glutathione affinity chromatography, or recombinant GST-tagged wild-type isozyme GAD65 from Escherichia coli strain BL21 by glutathione affinity chromatography and cleavage of the GST-tag by PreScission protease cleavage
amylose resin column chromatography, glutathione Sepharose 4B resin column chromatography
-
glutathione sepharose 4B resin column chromatography and amylose resin column chromatography
-
isoform GAD65 and GAD67 expressed in Escherichia coli as fusion protein with glutathione-S-transferase and 6*His-tagged isoforms GAD65 and GAD67 expressed in Saccharomyces cerevisiae
-
large-scale purification of GAD65 and GAD67
-
partial
-
recombinant GST-tagged wild-type isozyme GAD67 from Escherichia coli strain DH5alpha by glutathione affinity chromatography and cleavage of the GST-tag by Factor Xa, followed by another step of glutathione affinity chromatography, or recombinant GST-tagged wild-type isozyme GAD67 from Escherichia coli strain BL21 by glutathione affinity chromatography and cleavage of the GST-tag by PreScission protease cleavage
recombinant tagged enzyme from Escherichia coli strain DH5alpha
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GAD65, recombinant expression of GST-tagged or MBP-fusion wild-type enzyme, a 1757-bp hGAD65 insert from the pET-5C plasmid subcloned into the pMAL-c2X protein fusion system, in Escherichia coli strain DH5alpha, 1.6fold higher hGAD65 activity of the purified MBP-tagged enzyme construct compared to GST-tagged enzyme
gene GAD65, recombinant expression of GST-tagged wild-type and mutant isozymes in Escherichia coli strain DH5alpha or strain BL21
6*His-tagged isoforms GAD65 and GAD67 expressed in Saccharomyces cerevisiae
-
a hybrid cDNA is created by fusing a cDNA for amino acids 1-101 of GAD67 to a human cDNA for amino acids 96-585 of GAD65. The recombinant rGAD67/65 protein is expressed in yeast and has equivalent immunoreactivity to mammalian brain GAD with diabetes sera
-
creation of a hybrid form of GAD consisting of amino acids 1-101 of the human GAD67 protein fused to amino acids 96-585 of the human GAD65 protein, and modification of this to include a C-terminal hexa-His tag sequence. The hybrid GAD67/65-H6 is expressed in two yeast hosts: constitutively under the control of the plasmid oxidase promoter PGK1 in Saccharomyces cerevisiae, and inducibly under the control of the chromosomal alcohol oxidase promoter AOX1 in Pichia pastoris. The hybrid GAD67/65 is isolated at high specific activity and moderate yield, and the addition of the His6 tag sequence of the choice of the yeast strain does not appreciably affect enzyme activity, percentage recovery of GAD, protein purification or utility in diagnosis of diabetes in terms of specificity and sensitivity to the various sera
-
expressed in Escherichia coli
-
expressed in Escherichia coli DH5alpha cells
-
expression as glutathione S-transferase-fusion protein
-
expression in Sacchaormyces cerevisiae, His-tag
-
Expression of aggregation-prone deletion mutant protein (amino acids 448-585) using RNA polymerase sigma factor (RpoS) or glutathione S-transferase as fusion partners in Escherichia coli strain BL21 (DE3).
-
expression of GAD65
-
expression of labeled GAD65 in CHO cells
-
expression of the full-length and truncated mutant enzymes, expression analysis
-
gene GAD1, genomic organization, the gene located within chromosome 2q31 encodes the isozyme GAD67
-
gene GAD65, recombinant expression of full-length human GAD65 in Chlamydomonas reinhardtii strain 137c chloroplast genome under the control of the Chlamydomonas reinhardtii chloroplast rbcL promoter and 5'- and 3'-UTRs by particle bombardment
-
gene GAD67, recombinant expression of GST-tagged wild-type isozyme in Escherichia coli strain DH5alpha or strain BL21
gene gadB, expression in Escherichia coli strain DH5alpha using plasmids pMAL-c2X and the pGEX-3X and fusion to the maltose binding protein or GST, cytoplasmic targeting, overview
-
genotyping and expression analysis of isozyme GAD1 and GAD2 genes in individuals from Ireland and North Ireland, detailed overview
-
GST-GAD fusion protein expressed in Escherichia coli
-
recombinant expression of isozyme GAD65 using the Spodoptera frugiperda transfection method
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
glutamic acid decarboxylase67 mRNA expression is decreased in multiple brain areas of patients with schizophrenia and mood disorders
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
the diabetes autoantibody standardization program, DASP, aims to improve and standardize measurement of autoantibodies, e.g. glutamic acid decarboxylase autoantibodies and islet antigen-2, against associated with type 1 diabetes, overview
diagnostics
medicine
pharmacology
-
the enzyme is a potential important marker for the prediction and diagnosis of type 1 diabetes, and for the development of antigen-specific therapies for the treatment of type 1 diabetes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Blindermann, J.M.; Maitre, M.; Ossola, L.; Mandel, P.
Purification and some properties of L-glutamate decarboxylase from human brain
Eur. J. Biochem.
86
143-152
1978
Homo sapiens
Manually annotated by BRENDA team
Davis, K.M.; Foos, T.; Bates, C.S.; Tucker, E.; Hsu, C.C.; Chen, W.; Jin, H.; Tyburski, J.B.; Schloss, J.V.; Tobin, A.J.; Wu, J.Y.
A novel method for expression and large-scale production of human brain l-glutamate decarboxylase
Biochem. Biophys. Res. Commun.
267
777-782
2000
Homo sapiens
Manually annotated by BRENDA team
Primo, M.E.; Anton, E.A.; Villanueva, A.L.; Poskus, E.; Ermacora, M.R.
Engineered variants of human glutamic acid decarboxylase (GAD) and autoantibody epitope recognition
Clin. Immunol.
108
38-45
2003
Homo sapiens
Manually annotated by BRENDA team
Papakonstantinou, T.; Law, R.H.P.; Gardiner, P.; Rowley, M.J.; Mackay, I.R.
Comparative expression and purification of human glutamic acid decarboxylase from Saccharomyces cerevisiae and Pichia pastoris
Enzyme Microb. Technol.
26
645-652
2000
Homo sapiens
Manually annotated by BRENDA team
Davis, K.; Foos, T.; Wu, J.Y.; Schloss, J.V.
Oxygen-induced seizures and inhibition of human glutamate decarboxylase and porcine cysteine sulfinic acid decarboxylase by oxygen and nitric oxide
J. Biomed. Sci.
8
359-364
2001
Homo sapiens
Manually annotated by BRENDA team
Tong, J.C.; Mackay, I.R.; Chin, J.; Law, R.H.; Fayad, K.; Rowley, M.J.
Enzymatic characterization of a recombinant isoform hybrid of glutamic acid decarboxylase (rGAD67/65) expressed in yeast
J. Biotechnol.
97
183-190
2002
Homo sapiens
Manually annotated by BRENDA team
Buss, K.; Drewke, C.; Lohmann, S.; Piwonska, A.; Leistner, E.
Properties and interaction of heterologously expressed glutamate decarboxylase isoenzymes GAD(65kDa) and GAD(67kDa) from human brain with ginkgotoxin and its 5'-phosphate
J. Med. Chem.
44
3166-3174
2001
Homo sapiens
Manually annotated by BRENDA team
Zanone, M.M.; Catalfamo, E.; Pietropaolo, S.L.; Rabbone, I.; Sacchetti, C.; Cerutti, F.; Trucco, M.; Cavallo-Perin, P.
Glutamic acid decarboxylase and ICA512/IA-2 autoantibodies as disease markers and relationship to residual beta-cell function and glycemic control in young type 1 diabetic patients
Metabolism
52
25-29
2003
Homo sapiens
Manually annotated by BRENDA team
Lappalainen, J.; Sanacora, G.; Kranzler, H.R.; Malison, R.; Hibbard, E.S.; Price, L.H.; Krystal, J.; Gelernter, J.
Mutation screen of the glutamate decarboxylase-67 gene and haplotype association to unipolar depression
Am. J. Med. Genet.
124
81-86
2004
Homo sapiens
Manually annotated by BRENDA team
Wei, J.; Davis, K.M.; Wu, H.; Wu, J.Y.
Protein phosphorylation of human brain glutamic acid decarboxylase (GAD)65 and GAD67 and its physiological implications
Biochemistry
43
6182-6189
2004
Homo sapiens
Manually annotated by BRENDA team
Sha, D.; Wei, J.; Wu, H.; Jin, Y.; Wu, J.Y.
Molecular cloning, expression, purification, and characterization of shorter forms of human glutamic decarboxylase 67 in an E. coli expression system
Brain Res. Mol. Brain Res.
136
255-261
2005
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Jin, H.; Sha, D.; Wei, J.; Davis, K.M.; Wu, H.; Jin, Y.; Wu, J.Y.
Effect of apocalmodulin on recombinant human brain glutamic acid decarboxylase
J. Neurochem.
92
739-748
2005
Homo sapiens
Manually annotated by BRENDA team
Ma, S.; Huang, Y.; Yin, Z.; Menassa, R.; Brandle, J.E.; Jevnikar, A.M.
Induction of oral tolerance to prevent diabetes with transgenic plants requires glutamic acid decarboxylase (GAD) and IL-4
Proc. Natl. Acad. Sci. USA
101
5680-5685
2004
Homo sapiens
Manually annotated by BRENDA team
Sardana, R.K.; Awad, R.; Arnason, J.T.; Trudeau, V.L.
Expression of recombinant goldfish glutamic acid decarboxylase 65 and evidence for differential pH and PLP responsiveness compared to the human enzyme
Comp. Biochem. Physiol. B
144B
94-100
2006
Carassius auratus, Homo sapiens
-
Manually annotated by BRENDA team
Matsukawa, S.; Ueno, H.
Expression of glutamate decarboxylase isoform, GAD65, in human mononuclear leucocytes: a possible implication of C-terminal end deletion by Western blot and RT PCR study
J. Biochem.
142
633-638
2007
Homo sapiens
Manually annotated by BRENDA team
Fenalti, G.; Law, R.H.; Buckle, A.M.; Langendorf, C.; Tuck, K.; Rosado, C.J.; Faux, N.G.; Mahmood, K.; Hampe, C.S.; Banga, J.P.; Wilce, M.; Schmidberger, J.; Rossjohn, J.; El-Kabbani, O.; Pike, R.N.; Smith, A.I.; Mackay, I.R.; Rowley, M.J.; Whisstock, J.C.
GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop
Nat. Struct. Mol. Biol.
14
280-286
2007
Homo sapiens
Manually annotated by BRENDA team
Park, J.S.; Han, K.Y.; Lee, J.H.; Song, J.A.; Ahn, K.Y.; Seo, H.S.; Sim, S.J.; Kim, S.W.; Lee, J.
Solubility enhancement of aggregation-prone heterologous proteins by fusion expression using stress-responsive Escherichia coli protein, RpoS
BMC Biotechnol.
8
15
2008
Homo sapiens
Manually annotated by BRENDA team
Wegner, N.; Wait, R.; Venables, P.J.
Evolutionarily conserved antigens in autoimmune disease: Implications for an infective aetiology
Int. J. Biochem. Cell Biol.
41
390-397
2008
Homo sapiens
Manually annotated by BRENDA team
Villalba, A.; Iacono, R.F.; Valdez, S.N.; Poskus, E.
Detection and immunochemical characterization of glutamic acid decarboxylase autoantibodies in patients with autoimmune diabetes mellitus
Autoimmunity
41
143-153
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Saiz, A.; Blanco, Y.; Sabater, L.; Gonzalez, F.; Bataller, L.; Casamitjana, R.; Ramio-Torrenta, L.; Graus, F.
Spectrum of neurological syndromes associated with glutamic acid decarboxylase antibodies: diagnostic clues for this association
Brain
131
2553-2563
2008
Homo sapiens
Manually annotated by BRENDA team
Rahmati, K.; Lernmark, A.; Becker, C.; Foltyn-Zadura, A.; Larsson, K.; Ivarsson, S.A.; Toern, C.
A comparison of serum and EDTA plasma in the measurement of glutamic acid decarboxylase autoantibodies (GADA) and autoantibodies to islet antigen-2 (IA-2A) using the RSR radioimmunoassay (RIA) and enzyme linked immunosorbent assay (ELISA) kits
Clin. Lab.
54
227-235
2008
Homo sapiens
Manually annotated by BRENDA team
Markakis, I.; Alexiou, E.; Xifaras, M.; Gekas, G.; Rombos, A.
Opsoclonus-myoclonus-ataxia syndrome with autoantibodies to glutamic acid decarboxylase
Clin. Neurol. Neurosurg.
110
619-621
2008
Homo sapiens
Manually annotated by BRENDA team
Toern, C.; Mueller, P.W.; Schlosser, M.; Bonifacio, E.; Bingley, P.J.; Bingley, P.J.
Diabetes antibody standardization program: evaluation of assays for autoantibodies to glutamic acid decarboxylase and islet antigen-2
Diabetologia
51
846-852
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kuo, P.H.; Kalsi, G.; Prescott, C.A.; Hodgkinson, C.A.; Goldman, D.; Alexander, J.; van den Oord, E.J.; Chen, X.; Sullivan, P.F.; Patterson, D.G.; Walsh, D.; Kendler, K.S.; Riley, B.P.
Associations of glutamate decarboxylase genes with initial sensitivity and age-at-onset of alcohol dependence in the irish affected Sib pair study of alcohol dependence
Drug Alcohol Depend.
101
80-87
2008
Homo sapiens
Manually annotated by BRENDA team
Yoshihara, A.; Isozaki, O.; Okubo, Y.; Takano, K.
Anti-glutamic acid decarboxylase antibody in Graves' disease is a possible indicator for the unlikelihood of going into remission with antithyroid agents
Endocr. J.
56
269-274
2009
Homo sapiens
Manually annotated by BRENDA team
Davies, H.; Mannan, S.; Brophy, S.; Williams, R.
Routine glutamic acid decarboxylase autoantibody (GADA) testing: patients perspective
Fam. Pract.
25
176-180
2008
Homo sapiens
Manually annotated by BRENDA team
Gos, T.; Guenther, K.; Bielau, H.; Dobrowolny, H.; Mawrin, C.; Truebner, K.; Brisch, R.; Steiner, J.; Bernstein, H.G.; Jankowski, Z.; Bogerts, B.
Suicide and depression in the quantitative analysis of glutamic acid decarboxylase-immunoreactive neuropil
J. Affect. Disord.
113
45-55
2009
Homo sapiens
Manually annotated by BRENDA team
Skorstad, G.; Hestvik, A.L.; Vartdal, F.; Holmoy, T.
Cerebrospinal fluid T cell responses against glutamic acid decarboxylase 65 in patients with stiff person syndrome
J. Autoimmun.
32
24-32
2008
Homo sapiens
Manually annotated by BRENDA team
Ledet, D.S.; Handgretinger, R.; Bertorini, T.E.; Hale, G.A.; Ribeiro, R.C.; Khan, R.B.
Leucoencephalopathy, transverse myelopathy, and peripheral neuropathy in association with glutamic acid decarboxylase-65 (GAD) antibodies in children with cancer
J. Child Neurol.
23
1357-1362
2008
Homo sapiens
Manually annotated by BRENDA team
Steed, J.; Gilliam, L.K.; Harris, R.A.; Lernmark, A.; Hampe, C.S.
Antigen presentation of detergent-free glutamate decarboxylase (GAD65) is affected by human serum albumin as carrier protein
J. Immunol. Methods
334
114-121
2008
Homo sapiens
Manually annotated by BRENDA team
Buttenschoen, H.N.; Lauritsen, M.B.; Daoud, A.E.; Hollegaard, M.; Jorgensen, M.; Tvedegaard, K.; Hougaard, D.; Boerglum, A.; Thorsen, P.; Mors, O.
A population-based association study of glutamate decarboxylase 1 as a candidate gene for autism
J. Neural Transm.
116
381-388
2009
Homo sapiens
Manually annotated by BRENDA team
Mata, S.; Muscas, G.C.; Naldi, I.; Rosati, E.; Paladini, S.; Cruciatti, B.; Bisulli, F.; Paganini, M.; Mazzi, G.; Sorbi, S.; Tinuper, P.
Non-paraneoplastic limbic encephalitis associated with anti-glutamic acid decarboxylase antibodies
J. Neuroimmunol.
199
155-159
2008
Homo sapiens
Manually annotated by BRENDA team
Ishida, K.; Mitoma, H.; Mizusawa, H.
Reversibility of cerebellar GABAergic synapse impairment induced by anti-glutamic acid decarboxylase autoantibodies
J. Neurol. Sci.
271
186-190
2008
Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Awad, R.; Crump, K.; Mullally, M.; Sardana, R.K.; Arnason, J.T.; Trudeau, V.L.
An improved method for production of recombinant human glutamic acid decarboxylase 65 for use in phytopharmaceutical assessment
Pharm. Biol.
46
72-81
2008
Homo sapiens
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Oak, S.; Gilliam, L.K.; Landin-Olsson, M.; Toern, C.; Kockum, I.; Pennington, C.R.; Rowley, M.J.; Christie, M.R.; Banga, J.P.; Hampe, C.S.
The lack of anti-idiotypic antibodies, not the presence of the corresponding autoantibodies to glutamate decarboxylase, defines type 1 diabetes
Proc. Natl. Acad. Sci. USA
105
5471-5476
2008
Homo sapiens
Manually annotated by BRENDA team
Liimatainen, S.; Peltola, M.; Sabater, L.; Fallah, M.; Kharazmi, E.; Haapala, A.M.; Dastidar, P.; Knip, M.; Saiz, A.; Peltola, J.
Clinical significance of glutamic acid decarboxylase antibodies in patients with epilepsy
Epilepsia
51
760-767
2010
Homo sapiens
Manually annotated by BRENDA team
Thompson, M.; Weickert, C.S.; Wyatt, E.; Webster, M.J.
Decreased glutamic acid decarboxylase67 mRNA expression in multiple brain areas of patients with schizophrenia and mood disorders
J. Psychiatr. Res.
43
970-977
2009
Homo sapiens (Q99259)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Awad, R.; Crump, K.; Mullally, M.; Sardana, R.K.; Arnason, J.T.; Trudeau, V.L.
An improved method for production of recombinant human glutamic acid decarboxylase 65 for use in phytopharmaceutical assessment
Pharm. Biol.
46
72-81
2008
Homo sapiens (Q05329)
-
Manually annotated by BRENDA team