Literature summary for 4.1.1.15 extracted from

Chu, W.C.; Metzler, D.E.
Enzymatically active truncated cat brain glutamate decarboxylase: expression, purification, and absorption spectrum (1994), Arch. Biochem. Biophys., 313, 287-295.

Search for more literature for 4.1.1.15

Cloned(Commentary)

Cloned (Comment)	Organism
truncated enzyme, recloned into the Escherichia coli expression vector pET11a, the N-terminal 77-84 amino acid residues encoded by the cloned gene have been deleted	Felis catus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.6	-	L-Glu	pH 7.8	Felis catus
1.37	-	L-Glu	-	Felis catus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
59000	-	2 * 59000, SDS-PAGE	Felis catus
110000	-	nondenaturing PAGE	Felis catus

Organism

Organism	UniProt	Comment	Textmining
Felis catus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Felis catus

Source Tissue

Source Tissue	Comment	Organism	Textmining
brain	-	Felis catus	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
3.25	-	-	Felis catus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Glu	-	Felis catus	4-Aminobutanoate + CO2	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 59000, SDS-PAGE	Felis catus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
7	-	L-Glu	-	Felis catus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.6	-	-	Felis catus

pH Range

pH Minimum	pH Maximum	Comment	Organism
5.2	7.8	pH 5.2: about 55% of maximal activity, pH 7.8: about 35% of maximal activity	Felis catus

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Release 2023.1 (January 2023)