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Literature summary for 1.4.1.13 extracted from

  • Mäntsälä, P.; Zalkin, H.
    Properties of apoglutamate synthase and comparison with glutamate dehydrogenase (1976), J. Biol. Chem., 251, 3300-3305.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-Bromo-2-oxoglutarate
-
Escherichia coli
4-Iodoacetamidosalicylate inactivation is faster at pH 4.6 to 5.5 compared to pH 6.5 to 7.2 Escherichia coli
Bromopyruvate
-
Escherichia coli
iodoacetamide
-
Escherichia coli
p-chloromercuribenzoate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
NADPH NH3-dependent glutamate synthase and apoglutamate synthase Escherichia coli
0.24
-
2-oxoglutarate NH3-dependent glutamate synthase and apoglutamate synthase Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli
0.24
-
apoenzyme lacking flavin and non-heme iron, glutamine-dependent activity Escherichia coli
0.92
-
native enzyme, NH3-dependent activity Escherichia coli
4.45
-
apoenzyme lacking flavin and non-heme iron, NH3-dependent activity Escherichia coli
18.64
-
native enzyme, glutamine-dependent activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADPH + H+ both native and apoglutamate synthase catalyze NADP+ reduction at approximately 12% the rate of NADPH oxidation Escherichia coli L-glutamate + NADP+
-
r
additional information NH3-dependent activity is increased approximately 5fold in apoglutamate synthase lacking flavin and non-heme iron Escherichia coli ?
-
?
NH3 + 2-oxoglutarate + NADPH + H+
-
Escherichia coli L-glutamate + NADP+
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.4
-
for glutamate synthesis, NH3-dependent glutamate synthase and apoenzyme Escherichia coli
9.4
-
optimum for glutamate-dependent reduction of NADP+, NH3-dependent enzyme, apoglutamate synthase enzyme Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.86
-
p-chloromercuribenzoate
-
Escherichia coli