| Glutamate/Leucine/Phenylalanine/Valine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 thermotoga maritima glutamate dehydrogenase mutant n97d, g376k | |||||||||
| Identifiers | |||||||||
| Symbol | ELFV_dehydrog | ||||||||
| Pfam | PF00208 | ||||||||
| Pfam clan | CL0063 | ||||||||
| InterPro | IPR006096 | ||||||||
| PROSITE | PDOC00071 | ||||||||
| SCOP2 | 1leh / SCOPe / SUPFAM | ||||||||
| |||||||||
| Glu/Leu/Phe/Val dehydrogenase, dimerisation domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | ELFV_dehydrog_N | ||||||||
| Pfam | PF02812 | ||||||||
| SCOP2 | 1leh / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, the ELFV dehydrogenase family of enzymes include glutamate, leucine, phenylalanine and valine dehydrogenases. These enzymes 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. [1] [2] 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 [3] - 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. [4]
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. [5] 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 an NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate. [6]
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. [7]
These enzymes contain two domains, an N-terminal dimerisation domain, and a C-terminal domain. [8]