Domain

Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal (IPR006096)

Short name: Glu/Leu/Phe/Val_DH_C

Domain relationships

  • NAD(P)-binding domain (IPR016040)
    • Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal (IPR006096)

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 (EC:1.4.1.2, EC:1.4.1.3, and EC:1.4.1.4) (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].

Leucine dehydrogenase (EC:1.4.1.9) (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.

Phenylalanine dehydrogenase (EC:1.4.1.20) (PheDH) is na NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate [PMID: 1880121].

Valine dehydrogenase (EC:1.4.1.8) (ValDH) is an NADP-dependent enzyme that catalyses the reversible deamidation of L-valine into 3-methyl-2-oxobutanoate [PMID: 8320231].

This entry represents the C-terminal domain of these proteins.

GO terms

Biological Process

GO:0006520 cellular amino acid metabolic process
GO:0055114 oxidation-reduction process

Molecular Function

GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
SMART
Pfam