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Literature summary extracted from

  • Ruiz, J.L.; Ferrer, J.; Pire, C.; Llorca, F.I.; Bonete, M.J.
    Denaturation studies by fluorescence and quenching of thermophilic protein NAD+-glutamate dehydrogenase from Thermus thermophilus HB8 (2003), J. Protein Chem., 22, 295-301.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.4.1.2 Urea 72°C, maximal enhancement at 2 mM Thermus thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.2 guanidine hydrochloride 72°C, almost complete loss of activity by addition of more than 3 M Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.2 Thermus thermophilus
-
-
-
1.4.1.2 Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.4.1.2 after 10fold dilution of the enzyme denatured with 3 M guanidine hydrochloride, the enzyme does not recover its activity, whereas after dialysis, the protein recovers 10% of the original activity value Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.2 L-glutamate + H2O + NAD+
-
 Thermus thermophilus 2-oxoglutarate + NH3 + NADH + H+
-
 ?
1.4.1.2 L-glutamate + H2O + NAD+
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 2-oxoglutarate + NH3 + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.1.2 NAD+-glutamate dehydrogenase
-
 Thermus thermophilus
1.4.1.2 t-GDH
-
 Thermus thermophilus