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Literature summary extracted from

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

Activating Compound

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.15 Cycloglutamates
-
Escherichia coli
4.1.1.15 Substituted dicarboxylic acids
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.15 0.5 1.9 L-Glu at pH 4.6 Escherichia coli
4.1.1.15 0.6
-
L-Glu
-
Clostridium perfringens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.15 50000
-
6 * 50000 Escherichia coli
4.1.1.15 290000
-
-
Clostridium perfringens
4.1.1.15 310000
-
equilibrium sedimentation Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.15 Clostridium perfringens
-
-
-
4.1.1.15 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.15
-
Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.15 67.9
-
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.1.1.15 hexamer 6 * 50000 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.15 4 4.5
-
Escherichia coli
4.1.1.15 4.7
-
-
Clostridium perfringens

Cofactor

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