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Literature summary for 1.4.1.13 extracted from

  • Schreier, H.J.; Bernlohr, R.W.
    Purification and properties of glutamate synthase from Bacillus licheniformis (1984), J. Bacteriol., 160, 591-599.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
CaCl2 27% inhibition at 50 mM Bacillus licheniformis
DL-methionine sulfoxide potent inhibitor Bacillus licheniformis
glycine 5% inhibition at 5 mM Bacillus licheniformis
L-alanine 5% inhibition at 5 mM Bacillus licheniformis
L-histidine 5% inhibition at 5 mM Bacillus licheniformis
L-leucine 16% inhibition at 5 mM Bacillus licheniformis
L-methionine 16% inhibition at 5 mM Bacillus licheniformis
L-methionine DL-sulfoximine potent inhibitor Bacillus licheniformis
L-methionine sulfone potent inhibitor Bacillus licheniformis
L-serine 10% inhibition at 5 mM Bacillus licheniformis
MgCl2 31% inhibition at 50 mM Bacillus licheniformis
MnCl2 64% inhibition at 50 mM Bacillus licheniformis
additional information relatively insensitive to inhibition by amino acids, keto acids or various nucleotides, 38% inhibition with a combination of each 5 mM L-methionine, L-leucine, L-serine, L-histidine, L-glycine and L-alanine Bacillus licheniformis
NADP+ competitive inhibition with respect to NADPH; potent inhibitor Bacillus licheniformis
NADPH
-
Bacillus licheniformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
NADPH
-
Bacillus licheniformis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron iron-sulfur protein Bacillus licheniformis
Iron 8.1 iron atoms per MW 220000 Bacillus licheniformis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
1 * 158000 + 1 * 54000, SDS-PAGE Bacillus licheniformis
158000
-
1 * 158000 + 1 * 54000, SDS-PAGE Bacillus licheniformis
220000
-
sucrose density gradient sedimentation Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using streptomycin sulfate treatment, ammonium sulfate precipitation, column chromatography on DEAE-Sephacel, Bio-Gel A 1.5 m, Red Sepharose CL6B and Sephadex G-25 Bacillus licheniformis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
22.9
-
-
Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADPH + H+ highly specific Bacillus licheniformis L-glutamate + NADP+
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Bacillus licheniformis L-glutamate + NADP+
-
?

Subunits

Subunits Comment Organism
dimer 1 * 158000 + 1 * 54000, SDS-PAGE Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
glutamine-dependent activity Bacillus licheniformis
8.7
-
ammonia-dependent activity Bacillus licheniformis

Cofactor

Cofactor Comment Organism Structure
flavin ratio FAD: FMN is 1.2 Bacillus licheniformis
flavin 2 flavin moieties per 220000 MW Bacillus licheniformis
additional information the enzyme contains 8.1 acid-labile sulfur atoms per 220000-dalton dimer Bacillus licheniformis
NADPH
-
Bacillus licheniformis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.02
-
NADP competitive inhibition with NADPH Bacillus licheniformis