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Literature summary for 1.4.1.3 extracted from

  • Electricwala, A.H.; Dickinson, F.M.
    Kinetic studies of dogfish liver glutamate dehydrogenase (1979), Biochem. J., 177, 449-459.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
pyridoxal 5'-phosphate NAD+ and NADP+ protect from inactivation in the presence of sodium glutarate dogfish

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
300000 350000 liver, sedimentation equilibrium dogfish

Organism

Organism UniProt Comment Textmining
dogfish
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+ kinetic data suggest either a rapid-equilibrium random mechanism or a compulsory mechanism with binding sequence NH4+, NAD(P)H, 2-oxoglutarate dogfish

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
dogfish
-

Storage Stability

Storage Stability Organism
-15°, stable for several months dogfish

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + H2O + NAD(P)+
-
dogfish 2-oxoglutarate + NH3 + NAD(P)H
-
r

Cofactor

Cofactor Comment Organism Structure
NAD+
-
dogfish
NADP+
-
dogfish