InterPro domain: IPR014362

This entry represents glutamate dehydrogenases (GDH). The tertiary structure have been solved for the GDHs from Thermotoga maritima and Pyrococcus furiosus, both of which are thermostable because of an ion-pair network in the hinge region [ 1 ]. Some GDHs are NADP-specific, such as GdhA from Escherichia coli, which catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia [ 2 , 3 ]. In eukaryotes, NADP-dependent GDHs may be mitochondrial, such as GluD from Dictyostelium discoideum [ 4 ].

1. Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. I. Introduction of a six-residue ion-pair network in the hinge region. J. Mol. Biol. 280, 287-96
2. Glutamate dehydrogenase from Escherichia coli: induction, purification and properties of the enzyme. Biochim. Biophys. Acta 377, 217-28
3. Glutamate dehydrogenase from Escherichia coli: purification and properties. J. Bacteriol. 124, 775-83
4. The NAD-dependent glutamate dehydrogenase from Dictyostelium discoideum: purification and properties. Arch. Biochem. Biophys. 291, 225-30