InterPro domain: IPR033922

Glutamate dehydrogenase (DH) is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms [ 1 , 2 , 3 ]. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent [ 4 ]. This entry represents the C-terminal domain.

1. Insights into the molecular basis of thermal stability from the structure determination of Pyrococcus furiosus glutamate dehydrogenase. FEMS Microbiol. Rev. 18, 105-17
2. Large-scale domain movements and hydration structure changes in the active-site cleft of unligated glutamate dehydrogenase from Thermococcus profundus studied by cryogenic X-ray crystal structure analysis and small-angle X-ray scattering. Biochemistry 40, 3069-79
3. Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. Implications for nucleotide specificity. J. Mol. Biol. 228, 662-71
4. Regulation of human glutamate dehydrogenases: implications for glutamate, ammonia and energy metabolism in brain. J. Neurosci. Res. 66, 899-908