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Literature summary 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

EC Number Inhibitors Comment Organism Structure
1.4.1.3 ADP
-
 Bos taurus
1.4.1.3 GTP
-
 Bos taurus

Localization

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

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.3 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.3
-
 Bos taurus

Reaction

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.1.3 liver
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.1.3 0.00076
-
 activity in liver nuclei, cofactor NADH Bos taurus
1.4.1.3 0.0028
-
 activity in liver mitochondria, cofactor NADH Bos taurus
1.4.1.3 4.8
-
 enzyme purified from liver nuclei Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.3 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