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Literature summary for 4.1.1.15 extracted from

  • Johnson, B.S.; Singh, N.K.; Cherry, J.H.; Locy, R.D.
    Purification and characterization of glutamate decarboxylase from cowpea (1997), Phytochemistry, 46, 39-44.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
L-Glu substrate inhibition at high concentrations Vigna unguiculata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2
-
L-Glu
-
Vigna unguiculata

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ plus calmudulin, at pH 5.8, activates Vigna unguiculata

Organism

Organism UniProt Comment Textmining
Vigna unguiculata
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Vigna unguiculata

Source Tissue

Source Tissue Comment Organism Textmining
pod
-
Vigna unguiculata
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.57
-
-
Vigna unguiculata

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 6
-
Vigna unguiculata

pH Range

pH Minimum pH Maximum Comment Organism
4 6.5 pH 4.0: about 75% of maximal activity, pH 6.5: about 55% of maximal activity Vigna unguiculata

Cofactor

Cofactor Comment Organism Structure
Calmodulin plus Ca2+, at pH 5.8, activates Vigna unguiculata