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Literature summary for 1.4.1.2 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
Search for more literature for 1.4.1.2

Activating Compound

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

Inhibitors

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

Organism

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

Renatured (Commentary)

Renatured (Comment) Organism
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)

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

Synonyms

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