Phenylalanine dehydrogenase

From Wikipedia, the free encyclopedia

In enzymology, a phenylalanine dehydrogenase (EC 1.4.1.20) is an enzyme that catalyzes the chemical reaction

L-phenylalanine + H₂O + NAD⁺ $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1BW9 and 1BXG.

[edit] References

IUBMB entry for 1.4.1.20
BRENDA references for 1.4.1.20 (Recommended.)
PubMed references for 1.4.1.20
PubMed Central references for 1.4.1.20
Google Scholar references for 1.4.1.20
Asano Y, Nakazawa A, Endo K (1987). "Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization". J. Biol. Chem. 262: 10346–54. 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: 153–9. doi:10.1111/j.1432-1033.1987.tb13399.x. PMID 3311741.