3 Ontology Annotations
GO Term | Gene Name |
---|---|
GO:0016491 | IPR006095 |
GO:0006520 | IPR006095 |
GO:0055114 | IPR006095 |
Type: | Family | Name: | Glutamate/phenylalanine/leucine/valine dehydrogenase |
Description: | 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 (, , and ) (GluDH) are enzymes that catalyse the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate [, ]. 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 [] - 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 [].Leucine dehydrogenase () (LeuDH) is a NAD-dependent enzyme that catalyses the reversible deamination of leucine and several other aliphatic amino acids to their keto analogues []. Each subunit of this octameric enzyme from Bacillus sphaericuscontains 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.Phenylalanine dehydrogenase () (PheDH) is na NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate [].Valine dehydrogenase () (ValDH) is an NADP-dependent enzyme that catalyses the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate []. | Short Name: | Glu/Leu/Phe/Val_DH |
GO Term | Gene Name |
---|---|
GO:0016491 | IPR006095 |
GO:0006520 | IPR006095 |
GO:0055114 | IPR006095 |