Phenylalanine dehydrogenase

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

L-phenylalanine + H₂O + NAD⁺ ${\displaystyle \rightleftharpoons }$ 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.

Structural studies

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

References

• 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. 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.

This page was last edited on 26 August 2023, at 15:21