ELFV_dehydrogGlutamate/Leucine/Phenylalanine/Valine dehydrogenase |
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SMART accession number: | SM00839 |
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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) ]. In rice, glutamate dehydrogenase 3 is mitochondrial. 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: | cellular amino acid metabolic process (GO:0006520), oxidation-reduction process (GO:0055114) |
GO function: | oxidoreductase activity (GO:0016491) |
Family alignment: |
There are 30530 ELFV_dehydrog domains in 30511 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
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