Literature summary for 4.1.1.15 extracted from

Battaglioli, G.; Liu, H.; Hauer, C.R.; Martin, D.L.
Glutamate decarboxylase: loss of N-terminal segment does not affect homodimerization and determination of the oxidation state of cysteine residues (2005), Neurochem. Res., 30, 989-1001.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.18	-	L-glutamate	isoform GAD67, treated with trypsin, which also increases vmax value by 31%	Rattus norvegicus
0.3	-	L-glutamate	isoform GAD67	Rattus norvegicus
1.33	-	L-glutamate	isoform GAD65, treated with trypsin, which also increases vmax value by 33%	Rattus norvegicus
1.44	-	L-glutamate	isoform GAD65	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	isoforms GAD65 and GAD67, expression in Sf9/baculovirus system	-

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
More	N-terminal segments of both GAD65 and GAD67 are exposed and flexible	Rattus norvegicus

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Release 2023.1 (January 2023)