Literature summary for 4.1.1.15 extracted from

Giovannercole, F.; Merigoux, C.; Zamparelli, C.; Verzili, D.; Grassini, G.; Buckle, M.; Vachette, P.; De Biase, D.
On the effect of alkaline pH and cofactor availability in the conformational and oligomeric state of Escherichia coli glutamate decarboxylase (2017), Protein Eng. Des. Sel., 30, 235-244 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene gadB, recombinant expression of holoenzyme	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-glutamate	Escherichia coli	-	4-aminobutanoate + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P69910	-	-

Purification (Commentary)

Purification (Comment)	Organism
purification of recombinant holoenzyme, preparation of apoenzyme, and reconstitution with pyridoxal 5'-phosphate, overview	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamate	-	Escherichia coli	4-aminobutanoate + CO2	-	?

Subunits

Subunits	Comment	Organism
dimer	at alkaline pH	Escherichia coli
hexamer	-	Escherichia coli
More	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	Escherichia coli

Synonyms

Synonyms	Comment	Organism
GadB	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	PLP, plays a key role in the acquisition of a folding necessary for the canonical catalytic activity. Preparation of recombinant apoenzyme, and reconstitution with pyridoxal 5'-phosphate, overview	Escherichia coli

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Release 2023.1 (January 2023)