| 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. 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 - 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.
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. 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.
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.
These enzymes contain two domains, an N-terminal dimerisation domain, and a C-terminal domain.
References
- Britton KL, Baker PJ, Rice DW, Stillman TJ (November 1992). "Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases". Eur. J. Biochem. 209 (3): 851–9. doi:10.1111/j.1432-1033.1992.tb17357.x. PMID 1358610.
- Benachenhou-Lahfa N, Forterre P, Labedan B (April 1993). "Evolution of glutamate dehydrogenase genes: evidence for two paralogous protein families and unusual branching patterns of the archaebacteria in the universal tree of life". J. Mol. Evol. 36 (4): 335–46. doi:10.1007/bf00182181. PMID 8315654. S2CID 25117393.
- Moye WS, Amuro N, Rao JK, Zalkin H (July 1985). "Nucleotide sequence of yeast GDH1 encoding nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase". J. Biol. Chem. 260 (14): 8502–8. doi:10.1016/S0021-9258(17)39500-5. PMID 2989290.
- Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, Zannis V, Plaitakis A, Papamatheakis J, Moschonas N (May 1988). "Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family". Proc. Natl. Acad. Sci. U.S.A. 85 (10): 3494–8. doi:10.1073/pnas.85.10.3494. PMC 280238. PMID 3368458.
- Nagata S, Tanizawa K, Esaki N, Sakamoto Y, Ohshima T, Tanaka H, Soda K (December 1988). "Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases". Biochemistry. 27 (25): 9056–62. doi:10.1021/bi00425a026. PMID 3069133.
- Takada H, Yoshimura T, Ohshima T, Esaki N, Soda K (March 1991). "Thermostable phenylalanine dehydrogenase of Thermoactinomyces intermedius: cloning, expression, and sequencing of its gene". J. Biochem. 109 (3): 371–6. doi:10.1093/oxfordjournals.jbchem.a123388. PMID 1880121.
- Tang L, Hutchinson CR (July 1993). "Sequence, transcriptional, and functional analyses of the valine (branched-chain amino acid) dehydrogenase gene of Streptomyces coelicolor". J. Bacteriol. 175 (13): 4176–85. doi:10.1128/jb.175.13.4176-4185.1993. PMC 204847. PMID 8320231.
- Baker, P. J.; Turnbull, A. P.; Sedelnikova, S. E.; Stillman, T. J.; Rice, D. W. (1995). "A role for quaternary structure in the substrate specificity of leucine dehydrogenase". Structure. 3 (7): 693–705. doi:10.1016/S0969-2126(01)00204-0. PMID 8591046.