Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.15 3.2
-
L-Glu
-
Vigna unguiculata

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.15 Vigna unguiculata
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.15
-
Vigna unguiculata

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.1.1.15 pod
-
Vigna unguiculata
-

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 2.57
-
-
Vigna unguiculata

Substrates and Products (Substrate)

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.15 5.5 6
-
Vigna unguiculata

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.15 4 6.5 pH 4.0: about 75% of maximal activity, pH 6.5: about 55% of maximal activity Vigna unguiculata

Cofactor

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