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Literature summary for 4.1.1.15 extracted from

  • Wei, J.; Wu, J.Y.
    Post-translational regulation of L-glutamic acid decarboxylase in the brain (2008), Neurochem. Res., 33, 1459-1465.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C30A mutation of Cys30 to Ala abolishes the presynaptic clustering of GAD65 in primary hippocampal neurons Homo sapiens
C45A mutation of Cys30 to Ala abolishes the presynaptic clustering of GAD65 in primary hippocampal neurons Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
axon
-
Mus musculus 30424
-
axon
-
Rattus norvegicus 30424
-
axon
-
Homo sapiens 30424
-
endosome 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 Mus musculus 5768
-
endosome 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 Rattus norvegicus 5768
-
endosome 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 Homo sapiens 5768
-
Golgi membrane 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 Mus musculus 139
-
Golgi membrane 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 Rattus norvegicus 139
-
Golgi membrane 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 Homo sapiens 139
-
additional information GAD67 is evenly distributed throughout the cell Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate Homo sapiens 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 4-aminobutanoate + CO2
-
?
L-glutamate Mus musculus 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 4-aminobutanoate + CO2
-
?
L-glutamate Rattus norvegicus 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 4-aminobutanoate + CO2
-
?
L-glutamate Homo sapiens GAD is the rate-limiting enzyme in controlling GABA synthesis, GAD65 is transiently activated in response to the extra demand of GABA in neurotransmission 4-aminobutanoate + CO2
-
?
additional information Homo sapiens GAD65 plays an essential role in neurotransmission, and is a typical autoantigen in several human autoimmune diseases, such as insulin-dependent diabetes mellitus, IDDM and Stiffman-Person syndrome, SPS. Posttranslational regulation of the enzyme in brain, overview ?
-
?
additional information Mus musculus GAD65 plays an essential role in neurotransmission, overview ?
-
?
additional information Rattus norvegicus GAD65 plays an essential role in neurotransmission, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q05329 GAD65
-
Homo sapiens Q99259 GAD67
-
Mus musculus
-
-
-
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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 Mus musculus
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 Rattus norvegicus
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 Homo sapiens
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 Mus musculus
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 Rattus norvegicus
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 Homo sapiens
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 Mus musculus
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 Rattus norvegicus
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 Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Mus musculus
-
brain
-
Rattus norvegicus
-
brain
-
Homo sapiens
-
additional information GAD67 is evenly distributed throughout the cell Mus musculus
-
additional information GAD67 is evenly distributed throughout the cell Rattus norvegicus
-
additional information GAD67 is evenly distributed throughout the cell Homo sapiens
-
neuron
-
Mus musculus
-
neuron
-
Rattus norvegicus
-
neuron
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
Mus musculus 4-aminobutanoate + CO2
-
?
L-glutamate
-
Rattus norvegicus 4-aminobutanoate + CO2
-
?
L-glutamate
-
Homo sapiens 4-aminobutanoate + CO2
-
?
L-glutamate 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 Homo sapiens 4-aminobutanoate + CO2
-
?
L-glutamate 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 Mus musculus 4-aminobutanoate + CO2
-
?
L-glutamate 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 Rattus norvegicus 4-aminobutanoate + CO2
-
?
L-glutamate GAD is the rate-limiting enzyme in controlling GABA synthesis, GAD65 is transiently activated in response to the extra demand of GABA in neurotransmission Homo sapiens 4-aminobutanoate + CO2
-
?
additional information GAD65 plays an essential role in neurotransmission, and is a typical autoantigen in several human autoimmune diseases, such as insulin-dependent diabetes mellitus, IDDM and Stiffman-Person syndrome, SPS. Posttranslational regulation of the enzyme in brain, overview Homo sapiens ?
-
?
additional information GAD65 plays an essential role in neurotransmission, overview Mus musculus ?
-
?
additional information GAD65 plays an essential role in neurotransmission, overview Rattus norvegicus ?
-
?

Subunits

Subunits Comment Organism
More 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 Mus musculus
More 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 Rattus norvegicus
More 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 Homo sapiens

Synonyms

Synonyms Comment Organism
GAD
-
Mus musculus
GAD
-
Rattus norvegicus
GAD
-
Homo sapiens
GAD65
-
Mus musculus
GAD65
-
Rattus norvegicus
GAD65
-
Homo sapiens
GAD67
-
Mus musculus
GAD67
-
Rattus norvegicus
GAD67
-
Homo sapiens
Glutamic acid decarboxylase
-
Mus musculus
Glutamic acid decarboxylase
-
Rattus norvegicus
Glutamic acid decarboxylase
-
Homo sapiens
L-Glutamic acid decarboxylase
-
Mus musculus
L-Glutamic acid decarboxylase
-
Rattus norvegicus
L-Glutamic acid decarboxylase
-
Homo sapiens