4.1.1.15: glutamate decarboxylase
This is an abbreviated version!
For detailed information about glutamate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.15
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4.1.1.15
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gabaergic
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gamma-aminobutyric
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autoimmune
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autoantibody
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islet
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mellitus
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neurotransmitter
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synaptic
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hippocampus
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interneurons
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cortical
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autoantigens
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choline
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excitatory
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dorsal
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striatum
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insulin-dependent
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ventral
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seizure
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parvalbumin
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epilepsy
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beta-cell
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cholinergic
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glutamatergic
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synapses
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medial
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neurotransmission
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neurochemical
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substantia
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afferent
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postsynaptic
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c-peptide
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somata
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chat
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presynaptic
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antibody-positive
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autoreactive
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ketoacidosis
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bicuculline
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gaba-transaminase
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colliculus
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preoptic
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gaba-t
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calretinin
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rostral
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muscimol
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boutons
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reelin
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calbindin
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analysis
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synthesis
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pharmacology
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nutrition
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medicine
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food industry
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diagnostics
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glycinergic
- 4.1.1.15
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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
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glycinergic
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
4.1.1.15 glutamate decarboxylaseAdvanced search results
results (
results (Subunits
Subunits on EC 4.1.1.15 - glutamate decarboxylase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
hexamer
homodimer
homohexamer
monomer
tetramer
additional information
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x * 53755, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE
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x * 53755, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE
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x * 53540, sequence calculation, x * 54400, recombinant His-tagged enzyme, SDS-PAGE
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x * 53540, sequence calculation, x * 54400, recombinant His-tagged enzyme, SDS-PAGE
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x * 53522, sequence calculation, x * 50000, recombinant His-tagged enzyme, SDS-PAGE
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x * 53522, sequence calculation, x * 50000, recombinant His-tagged enzyme, SDS-PAGE
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?
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x * 66000, recombinant His-tagged enzyme, SDS-PAGE, x * 65986, sequence calculation
?
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x * 66000, recombinant His-tagged enzyme, SDS-PAGE, x * 65986, sequence calculation
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dimer
2 * 54000, inactive, recombinant His-tagged enzyme, SDS-PAGE
dimer
Levilactobacillus brevis IFO 12005
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2 * 54000, inactive, recombinant His-tagged enzyme, SDS-PAGE
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dimer
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2 * 44000, high speed equilibrium sedimentation after treatment with 6 M guanidine HCl and 0.1 M beta-mercaptoethanol
dimer
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dimer-forming interactions are mediated mainly by carboxyl-terminal domain
hexamer
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GadB is a trimer of dimers, in which monomers from each dimer belong to different layers, structure comparisons, overview
homohexamer
X-ray crystallography, 6 * 57066, amino acid sequence
homohexamer
hexamer composed of a trimer of dimers. Hexamerization strongly contributes to the stability of the enzyme
tetramer
4 * 54000, ammonium sulfate-activated, recombinant His-tagged enzyme, SDS-PAGE
tetramer
Lactobacillus brevis IFO12005 is dimeric in the inactive form and tetrameric in the active form
tetramer
Levilactobacillus brevis FO12005
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Lactobacillus brevis IFO12005 is dimeric in the inactive form and tetrameric in the active form
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tetramer
Levilactobacillus brevis IFO 12005
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4 * 54000, ammonium sulfate-activated, recombinant His-tagged enzyme, SDS-PAGE
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additional information
in solution AtGAD1 is in a dimer-hexamer equilibrium. Binding of Ca2+/CaM1 abolishes the dissociation of the AtGAD1 oligomer. The AtGAD1N-terminal domain is critical for maintaining the oligomeric state. Arg24 in the N-terminal domain is a key residue. The oligomeric state of AtGAD1 is highly responsive to a number of experimental parameters and may have functional relevance in vivo in the light of the biphasic regulation of AtGAD1 activity by pH and Ca2+/CaM1 in plant cells. Tryptic peptide mapping. Effect of pH on the dissociation of hexameric AtGAD1 in the pH range 6.0-8.0, overview. A flexible and exposed stretch spanning residues 1-24 is the minimum region required for assembly of hexamer
additional information
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in solution AtGAD1 is in a dimer-hexamer equilibrium. Binding of Ca2+/CaM1 abolishes the dissociation of the AtGAD1 oligomer. The AtGAD1N-terminal domain is critical for maintaining the oligomeric state. Arg24 in the N-terminal domain is a key residue. The oligomeric state of AtGAD1 is highly responsive to a number of experimental parameters and may have functional relevance in vivo in the light of the biphasic regulation of AtGAD1 activity by pH and Ca2+/CaM1 in plant cells. Tryptic peptide mapping. Effect of pH on the dissociation of hexameric AtGAD1 in the pH range 6.0-8.0, overview. A flexible and exposed stretch spanning residues 1-24 is the minimum region required for assembly of hexamer
additional information
at acidic pH, when the enzyme is maximally active, BmGadB is a hexamer
additional information
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at acidic pH, when the enzyme is maximally active, BmGadB is a hexamer
additional information
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at acidic pH, when the enzyme is maximally active, BmGadB is a hexamer
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additional information
homohexameric GadB forms a triple-helix bundle interdomain at acidic pH
additional information
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homohexameric GadB forms a triple-helix bundle interdomain at acidic pH
additional information
addition of pyridoxine does not influence the aggregation state of GAD
additional information
Escherichia coli GAD forms a hexamer at acidic pH which consists of three functional dimers. In each dimer there are some special residues from both subunits that contribute in the formation of potential active sites and promote the interaction between the enzyme, cofactor and substrate. The N- and C-terminal domains of each subunit play an important role in conformational changes through pH shift. These conformational changes lead to activation of the enzyme at acidic pH and vice versa. The N-terminal residues involve in dimerization and subsequent migration of GAD to cytoplasmic site of the inner. The C-terminal domain by entrancing into the active site is also responsible for autoinhibition of the enzyme at neutral pH
additional information
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Escherichia coli GAD forms a hexamer at acidic pH which consists of three functional dimers. In each dimer there are some special residues from both subunits that contribute in the formation of potential active sites and promote the interaction between the enzyme, cofactor and substrate. The N- and C-terminal domains of each subunit play an important role in conformational changes through pH shift. These conformational changes lead to activation of the enzyme at acidic pH and vice versa. The N-terminal residues involve in dimerization and subsequent migration of GAD to cytoplasmic site of the inner. The C-terminal domain by entrancing into the active site is also responsible for autoinhibition of the enzyme at neutral pH
additional information
in GadB, the dimer is the functional unit as each active site is made of amino acid residues that are provided by both monomers in the dimer. Structural organization of EcGadB in solution in the pH range 7.5-8.6, overview. Analysis by small angle X-ray scattering combined with size exclusion chromatography and analytical ultracentrifugation analysis shows that the compact and entangled EcGadB hexameric structure undergoes dissociation into dimers as pH alkalinizes. When pyridoxal 5'-phosphate is not present, the dimeric species is the most abundant in solution, though evidence for the occurrence of a likely tetrameric species is also obtained. Molecular modeling
additional information
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in GadB, the dimer is the functional unit as each active site is made of amino acid residues that are provided by both monomers in the dimer. Structural organization of EcGadB in solution in the pH range 7.5-8.6, overview. Analysis by small angle X-ray scattering combined with size exclusion chromatography and analytical ultracentrifugation analysis shows that the compact and entangled EcGadB hexameric structure undergoes dissociation into dimers as pH alkalinizes. When pyridoxal 5'-phosphate is not present, the dimeric species is the most abundant in solution, though evidence for the occurrence of a likely tetrameric species is also obtained. Molecular modeling
additional information
Escherichia coli K-12 / MG1655
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addition of pyridoxine does not influence the aggregation state of GAD
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additional information
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both isoform GAD65 and GAD67 in vivo build up a protein complex with apocalmodulin
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
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
additional information
sodium glutamate is essential for tetramer formation and its activation
additional information
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sodium glutamate is essential for tetramer formation and its activation
additional information
asymmetrical flow field-flow fractionation (AF4) provides molecular weight (MW) (or size)-based separation of dimer, hexamer, and aggregates of LbGadB, molecular modeling
additional information
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asymmetrical flow field-flow fractionation (AF4) provides molecular weight (MW) (or size)-based separation of dimer, hexamer, and aggregates of LbGadB, molecular modeling
additional information
Levilactobacillus brevis DSM 1269
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asymmetrical flow field-flow fractionation (AF4) provides molecular weight (MW) (or size)-based separation of dimer, hexamer, and aggregates of LbGadB, molecular modeling
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additional information
Levilactobacillus brevis IFO 12005
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sodium glutamate is essential for tetramer formation and its activation
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additional information
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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
additional information
the C-terminal extension of enzyme plays a role as a strong autoinhibitory domain. Truncation causes the enzyme to act constitutively, with higher activity than wild-type both in vitro and in vivo
additional information
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the C-terminal extension of enzyme plays a role as a strong autoinhibitory domain. Truncation causes the enzyme to act constitutively, with higher activity than wild-type both in vitro and in vivo
additional information
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N-terminal segments of both GAD65 and GAD67 are exposed and flexible
additional information
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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
additional information
the N-terminal amino acid sequence of GAD is NH2-MNEKLFREI
additional information
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the N-terminal amino acid sequence of GAD is NH2-MNEKLFREI
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