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Information on EC 4.1.1.15 - glutamate decarboxylase and Organism(s) Arabidopsis thaliana and UniProt Accession Q42521
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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: Arabidopsis thaliana
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
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-
-
-
ERT D1
-
-
-
-
GAD
-
-
-
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GAD-65
-
-
-
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GAD-67
-
-
-
-
GAD-alpha
-
-
-
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GAD-beta
-
-
-
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GAD-gamma
-
-
-
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GADCase
-
-
-
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gamma-Glutamate decarboxylase
-
-
-
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GDCase
-
-
-
-
Glutamic acid decarboxylase
-
-
-
-
Glutamic decarboxylase
-
-
-
-
L-Aspartate-alpha-decarboxylase
-
-
-
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L-Glutamate alpha-decarboxylase
-
-
-
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L-Glutamate decarboxylase
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-
-
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L-Glutamic acid decarboxylase
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-
-
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L-Glutamic decarboxylase
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-
-
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MGAD
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
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-
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
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Calmodulin
a unique feature of plant GAD is the presence of a calmodulin (CaM)-binding domain at its C-terminus. In plants, transient elevation of cytosolic Ca2+ in response to different types of stress is responsible for GAD activation via CaM
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
in plants, transient elevation of cytosolic Ca2+ in response to different types of stress is responsible for GAD activation via calmodulin. Binding of Ca2+/CaM1 abolishes the dissociation of the AtGAD1 oligomer
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Calmodulin
activates Gad1 in a unique way by relieving two C-terminal autoinhibition domains of adjacent active sites, forming a 393 kDa Gad-Ca2+/calmodulin complex with a 1:3 stoichiometry
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the fold type I family of PLP-enzymes
physiological function
compared to GADs from other organisms, plant GADs possess a unique feature, namely, the presence of a C-terminal calmodulin binding site (CaMBD). This characteristic confers plant GADs an additional regulatory mechanism by making them responsive to cytosolic calcium (Ca2+), thus revealing that at least two mechanisms exist, by which GAD activity can be stimulated in vitro and in vivo, namely, acidic pH and Ca2+/CaM. Transient elevation of cytosolic Ca2+ in response to different types of stress is responsible for GAD activation via CaM
additional information
additional information
hexamerization strongly contributes to the stability of the enzyme. Plant GADs possess four conserved basic residues in their first 24 N-terminal amino acid region (H5,H15, R21, and R24 in AtGAD1). Two of the four residues (H15 and R24) are located at the interfaces between dimeric units
additional information
-
hexamerization strongly contributes to the stability of the enzyme. Plant GADs possess four conserved basic residues in their first 24 N-terminal amino acid region (H5,H15, R21, and R24 in AtGAD1). Two of the four residues (H15 and R24) are located at the interfaces between dimeric units
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). DCE1_ARATH
502
0
57066
Swiss-Prot
Chloroplast (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
342000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homohexamer
additional information
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
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
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, X-ray diffraction structure determination and analysis
sitting drop vapor diffusion method, using 100 mM sodium acetate pH 5.5, 720 mM sodium formate, 9% (w/v) PEG 8000, and 9% (w/v) PEG 1000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K496A/K497A
the mutant displays a substantial loss of enzymatic activity, at the pH optimum, the activity of the double mutant is reduced about 3fold
R24A
site-directed mutagenesis of key residue Arg24 in the N-terminal domain to Ala prevents hexamer formation of enzyme AtGAD1 in solution. The dimeric mutant enzyme forms a stable hexamer in the presence of Ca2+/ CaM1
additional information
additional information
removal of the first 24 N-terminal residues of AtGAD1 dramatically affects oligomerization by producing a dimeric enzyme. The deleted mutant retains decarboxylase activity, highlighting the dimeric nature of the basic structural unit of AtGAD1. The dimeric mutant enzyme forms a stable hexamer in the presence of Ca2+/CaM1. Binding of Ca2+/CaM1 appears to restore the hexamer species, since the gel filtration profiles of the mutant AtGAD1-DELTA1-24-Ca2+/CaM1 complex shows the same elution volume of the AtGAD1-Ca2+/CaM1 complex across the entire pH range. The AtGAD1-DELTA1-24 enzyme shows decreased thermal stability compared with the wild-type form
additional information
-
removal of the first 24 N-terminal residues of AtGAD1 dramatically affects oligomerization by producing a dimeric enzyme. The deleted mutant retains decarboxylase activity, highlighting the dimeric nature of the basic structural unit of AtGAD1. The dimeric mutant enzyme forms a stable hexamer in the presence of Ca2+/CaM1. Binding of Ca2+/CaM1 appears to restore the hexamer species, since the gel filtration profiles of the mutant AtGAD1-DELTA1-24-Ca2+/CaM1 complex shows the same elution volume of the AtGAD1-Ca2+/CaM1 complex across the entire pH range. The AtGAD1-DELTA1-24 enzyme shows decreased thermal stability compared with the wild-type form
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
Gad1 is not completely inactive at physiological pH and its residual activity is essential for normal plant development
705157
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CaM agarose column chromatography and Superdex 200 gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gad1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gut, H.; Dominici, P.; Pilati, S.; Astegno, A.; Petoukhov, M.V.; Svergun, D.I.; Gruetter, M.G.; Capitani, G.
A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase
J. Mol. Biol.
392
334-351
2009
Arabidopsis thaliana (Q42521), Arabidopsis thaliana
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