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Literature summary for 4.1.1.15 extracted from

  • Fonda, M.L.
    L-Glutamate decarboxylase from bacteria (1985), Methods Enzymol., 113, 11-16.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Br- activates Escherichia coli
Cl- activates Escherichia coli
F- activates Escherichia coli
I- activates Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Cycloglutamates
-
Escherichia coli
Substituted dicarboxylic acids
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.5 1.9 L-Glu at pH 4.6 Escherichia coli
0.6
-
L-Glu
-
Clostridium perfringens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
6 * 50000 Escherichia coli
290000
-
-
Clostridium perfringens
310000
-
equilibrium sedimentation Escherichia coli

Organism

Organism UniProt Comment Textmining
Clostridium perfringens
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
67.9
-
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alpha-Methylglutamate
-
Escherichia coli ?
-
?
L-Glu
-
Escherichia coli 4-Aminobutanoate + CO2
-
?
L-Glu
-
Clostridium perfringens 4-Aminobutanoate + CO2
-
?

Subunits

Subunits Comment Organism
hexamer 6 * 50000 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4 4.5
-
Escherichia coli
4.7
-
-
Clostridium perfringens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate one molecule of pyridoxal 5'-phosphate is covalently bound to a lysyl residue Escherichia coli