4.1.1.15: glutamate decarboxylase

This is an abbreviated version!
For detailed information about glutamate decarboxylase, go to the full flat file.

Reaction

Synonyms

42 kDa biotin-coupled protein, 65 kDa glutamic acid decarboxylase, 67 kDa glutamic acid decarboxylase, Aspartate 1-decarboxylase, Aspartic alpha-decarboxylase, AtGAD1, BmGAD, BmGadB, BMI_II334, Cysteic acid decarboxylase, Decarboxylase, glutamate, ERT D1, GAD, GAD B, GAD-65, GAD-67, GAD-alpha, GAD-beta, GAD-gamma, GAD1, GAD2, GAD3, Gad56, GAD65, GAD67, GadA, GadB, GADB1, gadB2, GADbeta, GADCase, gadlbhye1, gamma-Glutamate decarboxylase, GDC, GDCase, Glt decarboxylase, glutamate decarboxylase, glutamate decarboxylase 1, glutamate decarboxylase 65, glutamate decarboxylase 67, glutamate decarboxylase A, glutamate decarboxylase B, Glutamic acid decarboxylase, glutamic acid decarboxylase 65, glutamic acid decarboxylase 67, glutamic acid decarboxylase-65, glutamic acid decarboxylase-67, glutamic acid decarboxylase67, Glutamic decarboxylase, hGAD65, hGAD67, L-Aspartate-alpha-decarboxylase, L-glutamate 1-carboxylyase, L-Glutamate alpha-decarboxylase, L-Glutamate decarboxylase, L-glutamate decarboxylase 65, L-glutamate decarboxylase 67, L-Glutamic acid decarboxylase, L-Glutamic decarboxylase, LbGAD, LbGadB, MGAD, More, p42, PF1159, PfGAD, ScGAD, sll1641

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.1 Carboxy-lyases

                4.1.1.15 glutamate decarboxylase

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Results	in table
47	Activating Compound
10154	AA Sequence
39	Application
1	CAS Registry Number
96	Cloned(Commentary)
100	Cofactor
7	Crystallization (Commentary)
7114	Disease/ Diagnostics
10	Expression
83	General Information
9	General Stability
184	IC50 Value
381	Inhibitors
12	kcat/KM [mM/s]
4	Ki Value [mM]
91	KM Value [mM]
61	Localization
45	Metals/Ions
94	Molecular Weight [Da]
152	Natural Substrates/ Products (Substrates)
465	Organism
12	Pathway
90	PDB ID
74	pH Optimum
27	pH Range
15	pH Stability
13	pI Value
18	Posttranslational Modification
180	Protein Variants
70	Purification (Commentary)
2	Reaction
3	Reaction Type
254	Reference
207	Source Tissue
54	Specific Activity [micromol/min/mg]
5	Storage Stability
286	Substrates and Products (Substrate)
113	Subunits
366	Synonyms
1	Systematic Name
58	Temperature Optimum [°C]
13	Temperature Range [°C]
46	Temperature Stability [°C]
23	Turnover Number [1/s]

Posttranslational Modification

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of the Enzyme Summary Page.

Posttranslational Modification on EC 4.1.1.15 - glutamate decarboxylase

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

lipoprotein

3 entries

phosphoprotein

8 entries

proteolytic modification

6 entries

additional information

Homo sapiens

-

the enzyme undergoes posttranslational processing

695971

lipoprotein

Homo sapiens

Q05329, Q99259

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

700429

lipoprotein

Mus musculus

-

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

700429

lipoprotein

Rattus norvegicus

-

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

700429

phosphoprotein

Homo sapiens

-

isoform GAD65 is activated by phosphorylation, GAD67 is inhibited by phosphorylation. Phosphorylation of GAD67 occurs at T91

664038

phosphoprotein

Homo sapiens

Q05329, Q99259

protein kinase A is responsible for phosphorylation and inhibition of GAD67 activity, while calcineurin is the phosphatase responsible for dephosphorylation and activation of GAD67

700429

phosphoprotein

Homo sapiens

Q05329, Q99259

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

748691

phosphoprotein

Homo sapiens

Q05329, Q99259

isozyme GAD65 is activated by phosphorylation, while isozyme GAD67 is inhibited by phosphorylation. 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

748691

phosphoprotein

Mus musculus

-

protein kinase A is responsible for phosphorylation and inhibition of GAD67 activity, while calcineurin is the phosphatase responsible for dephosphorylation and activation of GAD67

700429

phosphoprotein

Rattus norvegicus

-

protein kinase A is responsible for phosphorylation and inhibition of GAD67 activity, while calcineurin is the phosphatase responsible for dephosphorylation and activation of GAD67

700429

phosphoprotein

Rattus norvegicus

Q05683

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

748691

phosphoprotein

Rattus norvegicus Sprague Dawley

-

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

-

proteolytic modification

Homo sapiens

Q05329, Q99259

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

700429

proteolytic modification

Homo sapiens

-

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

697040

proteolytic modification

Mus musculus

-

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

700429

proteolytic modification

Mus musculus

-

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

697040

proteolytic modification

Rattus norvegicus

-

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

700429

proteolytic modification

Rattus norvegicus

-

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

697040