Phenylalanine dehydrogenase
| phenylalanine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.1.20 | ||||||||
| CAS no. | 69403-12-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a phenylalanine dehydrogenase (EC 1.4.1.20) is an enzyme that catalyzes the chemical reaction
- L-phenylalanine + H2O + NAD+ phenylpyruvate + NH3 + NADH + H+
The 3 substrates of this enzyme are L-phenylalanine, H2O, and NAD+, whereas its 4 products are phenylpyruvate, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-phenylalanine:NAD+ oxidoreductase (deaminating). Other names in common use include L-phenylalanine dehydrogenase, and PHD. This enzyme participates in phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis.
Structural studies
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1BW9 and 1BXG.
References
[edit]- Asano Y, Nakazawa A, Endo K (1987). "Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization". J. Biol. Chem. 262 (21): 10346–54. doi:10.1016/S0021-9258(18)61119-6. PMID 3112142.
- Asano Y, Nakazawa A, Endo K, Hibino Y, Ohmori M, Numao N, Kondo K (1987). "Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning". Eur. J. Biochem. 168 (1): 153–9. doi:10.1111/j.1432-1033.1987.tb13399.x. PMID 3311741.
