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Literature summary extracted from

  • Perez-Pomares, F.; Ferrer, J.; Camacho, M.; Pire, C.; LLorca, F.; Bonete, M.J.
    Amino acid residues involved in the catalytic mechanism of NAD-dependent glutamate dehydrogenase from Halobacterium salinarum (1999), Biochim. Biophys. Acta, 1426, 513-525.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.2 diethyl dicarbonate inactivation follows pseudo-first-order kinetics Halobacterium salinarum
1.4.1.2 ethyl acetimidate inactivation with ethyl acetimidate shows pseudo-first-order kinetics Halobacterium salinarum
1.4.1.2 Glutarate competitive inhibitor Halobacterium salinarum
1.4.1.2 Tetranitromethane rapid loss of enzymatic activity versus time at various concentrations of modifier, showing pseudo-first-order kinetics Halobacterium salinarum

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.2 Halobacterium salinarum
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.2 L-glutamate + H2O + NAD+ proposed mechanism involves hydrogen binding of each of the two carboxylic groups to tyrosyl residues. Histidine interacts with one of the N-hydrogens of the L-glutamate amino group Halobacterium salinarum 2-oxoglutarate + NH3 + NADH + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.1.2 NAD-dependent glutamate dehydrogenase
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 Halobacterium salinarum