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Literature summary for 1.4.1.13 extracted from

  • Mäntsälä, P.; Zalkin, H.
    Glutamate synthase. Properties of the glutamine-dependent activity (1976), J. Biol. Chem., 251, 3294-3299.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-Bromo-2-oxoglutarate
-
Escherichia coli
4-Iodoacetamidosalicylate
-
Escherichia coli
Bromopyruvate
-
Escherichia coli
iodoacetamide selective inactivation of glutamine-dependent activity Escherichia coli
L-2-Amino-4-oxo-5-chloropentanoic acid selective inhibitor of glutamine-dependent activity Escherichia coli
N-ethylmaleimide
-
Escherichia coli
NADPH inactivation of glutamine-dependent activity, 50% inactivation at 0.36 mM in 10 min Escherichia coli
p-chloromercuribenzoate
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using streptomycin sulfate treatment, ammonium sulfate fractionation, heat treatment, agarose gel filtration and DEAE-cellulose column chromatography Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
14.3
-
native enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Escherichia coli L-glutamate + NADP+
-
?
NH3 + 2-oxoglutarate + NADPH + H+ the specific activity of native enzyme using NH3 varies between 5% and 7% of the glutamine-dependent activity Escherichia coli L-glutamate + NADP+
-
?

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.025
-
L-2-Amino-4-oxo-5-chloropentanoic acid
-
Escherichia coli