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Literature summary for 1.4.1.3 extracted from

  • Di Prisco, G.; Garofano, F.
    Purification and some properties of glutamate dehydrogenase from ox liver nuclei (1974), Biochem. Biophys. Res. Commun., 58, 683-689.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
Bos taurus
GTP
-
Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
Bos taurus 5634
-

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Reaction

Reaction Comment Organism Reaction ID
L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+ compulsory order mechanism at pH 8.8 Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00076
-
activity in liver nuclei, cofactor NADH Bos taurus
0.0028
-
activity in liver mitochondria, cofactor NADH Bos taurus
4.8
-
enzyme purified from liver nuclei Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + H2O + NAD(P)+ rate of glutamate synthesis is several-fold higher than the rate for the reverse reaction Bos taurus 2-oxoglutarate + NH3 + NAD(P)H
-
r