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  • ELFV_dehydrog

    Glutamate/Leucine/Phenylalanine/Valine dehydrogenase
    ELFV_dehydrog
    SMART accession number:SM00839
    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.
    Interpro abstract (IPR006096):

    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 [(PUBMED:1358610), (PUBMED: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 [(PUBMED: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 [(PUBMED: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 [(PUBMED: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 [(PUBMED: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 [(PUBMED:8320231)].

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

    GO process:oxidation-reduction process (GO:0055114), cellular amino acid metabolic process (GO:0006520)
    GO function:oxidoreductase activity (GO:0016491)
    Family alignment:
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    There are 7977 ELFV_dehydrog domains in 7968 proteins in SMART's nrdb database.

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