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Literature summary for 1.4.1.13 extracted from

  • Hemmilä, I.A.; Mäntsälä, P.I.
    Purification and properties of glutamate synthase and glutamate dehydrogenase from Bacillus megaterium (1978), Biochem. J., 173, 45-52.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
dimethyl suberimidate increases NH3-dependent activity Priestia megaterium

Inhibitors

Inhibitors Comment Organism Structure
dimethyl suberimidate inactivates glutamine-dependent activity Priestia megaterium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0071
-
NADPH
-
Priestia megaterium
0.009
-
2-oxoglutarate
-
Priestia megaterium
0.2
-
L-glutamine
-
Priestia megaterium
22
-
NH4Cl
-
Priestia megaterium

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
x * 142000 + x * 55000, SDS-PAGE Priestia megaterium
142000
-
x * 142000 + x * 55000, SDS-PAGE Priestia megaterium
840000
-
sucrose density-gradient centrifugation Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using streptomycin sulfate treatment, ammonium sulfate precipitation, column chromatography on Ultrogel AcA 22 and DEAE-Sephadex A-50, ultrafiltration with an Amicon PM 30 membrane and chromatography on hydroxyapatite column Priestia megaterium

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
23.8
-
-
Priestia megaterium

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 Priestia megaterium L-glutamate + NADP+
-
?
NH3 + 2-oxoglutarate + NADPH + H+ 2% to 4% relative activity to L-glutamine Priestia megaterium L-glutamate + NADP+
-
?

Subunits

Subunits Comment Organism
? x * 142000 + x * 55000, SDS-PAGE Priestia megaterium

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Priestia megaterium