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Literature summary extracted from

  • Matsuoka, K.; Kimura, K.
    Glutamate synthase from Bacillus subtilis PCI 219 (1986), J. Biochem., 99, 1087-1100.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.13 DL-methionine DL-sulfoximine
-
Bacillus subtilis
1.4.1.13 fumarate potent inhibitor of the glutamine-dependent activity Bacillus subtilis
1.4.1.13 L-glutamate noncompetitive inhibitor with respect to both 2-oxoglutarate and L-glutamine Bacillus subtilis
1.4.1.13 L-malate potent inhibitor of the glutamine-dependent activity Bacillus subtilis
1.4.1.13 L-methionine DL-sulfoximine inhibits the glutamine-dependent reaction Bacillus subtilis
1.4.1.13 NAD+ competitive inhibition with NADH, noncompetitive inhibition with 2-oxoglutarate or L-glutamine Bacillus subtilis
1.4.1.13 NADP+ competitive inhibition with NADPH, noncompetitive inhibition with 2-oxoglutarate or L-glutamine Bacillus subtilis
1.4.1.13 p-chloromercuribenzoate inhibits the glutamine-dependent reaction Bacillus subtilis
1.4.1.13 pyridoxal-5'-phosphate 52% inhibition of the glutamine-dependent reaction at 5 mM Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.13 0.006
-
NADPH in the presence of a fixed concentration of L-glutamine, and varied concentrations of alpha-ketoglutarate Bacillus subtilis
1.4.1.13 0.007
-
NADPH in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of L-glutamine Bacillus subtilis
1.4.1.13 0.007
-
alpha-ketoglutarate in the presence of a fixed concentration of NADPH, and varied concentrations of L-glutamine Bacillus subtilis
1.4.1.13 0.01
-
alpha-ketoglutarate in the presence of a fixed concentration of NADH, and varied concentrations of L-glutamine Bacillus subtilis
1.4.1.13 0.012
-
alpha-ketoglutarate in the presence of a fixed concentration of L-glutamine, and varied concentrations of NADH Bacillus subtilis
1.4.1.13 0.013
-
alpha-ketoglutarate in the presence of a fixed concentration of L-glutamine, and varied concentrations of NADPH Bacillus subtilis
1.4.1.13 0.091
-
NADH in the presence of a fixed concentration of L-glutamine, and varied concentrations of alpha-ketoglutarate Bacillus subtilis
1.4.1.13 0.102
-
L-glutamine in the presence of a fixed concentration of NADPH, and varied concentrations of alpha-ketoglutarate Bacillus subtilis
1.4.1.13 0.108
-
L-glutamine in the presence of a fixed concentration of NADH, and varied concentrations of alpha-ketoglutarate Bacillus subtilis
1.4.1.13 0.113
-
NADH in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of L-glutamine Bacillus subtilis
1.4.1.13 0.115
-
L-glutamine in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of NADPH Bacillus subtilis
1.4.1.13 0.12
-
L-glutamine in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of NADH Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.1.13 Iron iron-sulfur protein Bacillus subtilis
1.4.1.13 Iron 7.4 g-atoms of non-heme iron per mol of enzyme Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.13 56000
-
1 * 160000 + 1 * 56000 Bacillus subtilis
1.4.1.13 160000
-
1 * 160000 + 1 * 56000 Bacillus subtilis
1.4.1.13 210000
-
sucrose density sedimentation Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.13 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.13
-
Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
1.4.1.13 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+ mechanism Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.13 L-glutamine + 2-oxoglutarate + NADH + H+
-
Bacillus subtilis L-glutamate + NAD+
-
r
1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+
-
Bacillus subtilis L-glutamate + NADP+
-
?
1.4.1.13 NH3 + 2-oxoglutarate + NADPH + H+ 24% relative activity to L-glutamine with NADPH as electron donor and 6.3% relative activity to L-glutamine with NADH as electron donor Bacillus subtilis L-glutamate + NADP+
-
?

Subunits

EC Number Subunits Comment Organism
1.4.1.13 dimer 1 * 160000 + 1 * 56000 Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.13 6.9
-
NADH-glutamine dependent activity Bacillus subtilis
1.4.1.13 7.8
-
NADPH-glutamine dependent activity Bacillus subtilis
1.4.1.13 9.4
-
NADPH-NH3 dependent activity Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.13 flavin 0.83 mol of FMN and 0.81 mol of FAD per mol of enzyme Bacillus subtilis
1.4.1.13 additional information the enzyme contains 8.7 g atoms per mol Bacillus subtilis
1.4.1.13 NADH 21% relative activity to NADPH Bacillus subtilis
1.4.1.13 NADPH
-
Bacillus subtilis