Glutamate/phenylalanine/leucine/valine dehydrogenase (IPR006095)
Short name: Glu/Leu/Phe/Val_DH
Overlapping homologous superfamilies
- NAD(P)-binding domain superfamily (IPR036291)
- Glutamate/phenylalanine/leucine/valine dehydrogenase (IPR006095)
- Glutamate dehydrogenase (IPR014362)
- Glutamate/phenylalanine/leucine/valine dehydrogenase, bacterial/archaeal (IPR016211)
Glutamate, leucine, phenylalanine and valine dehydrogenases are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction.
Glutamate dehydrogenases (EC:18.104.22.168, EC:22.214.171.124, and EC:126.96.36.199) (GluDH) are enzymes that catalyse the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate [PMID: 1358610, PMID: 8315654]. GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism. Two separate enzymes are present in yeasts: the NADP-dependent enzyme, which catalyses the amination of alpha-ketoglutarate to L-glutamate; and the NAD-dependent enzyme, which catalyses the reverse reaction [PMID: 2989290] - this form links the L-amino acids with the Krebs cycle, which provides a major pathway for metabolic interconversion of alpha-amino acids and alpha- keto acids [PMID: 3368458]. In rice, glutamate dehydrogenase 3 is mitochondrial.
Leucine dehydrogenase (EC:188.8.131.52) (LeuDH) is a NAD-dependent enzyme that catalyses the reversible deamination of leucine and several other aliphatic amino acids to their keto analogues [PMID: 3069133]. Each subunit of this octameric enzyme from Bacillus sphaericus contains 364 amino acids and folds into two domains, separated by a deep cleft. The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle.
- PR00082 (GLFDHDRGNASE)