|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 22.214.171.124, EC 126.96.36.199, and EC 188.8.131.52) (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 184.108.40.206) (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.
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)|
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Literature (relevant references for this domain)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)