Phenylalanine dehydrogenase

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

The three substrates of this enzyme are L-phenylalanine, water, and oxidised nicotinamide adenine dinucleotide (NAD⁺). Its products are phenylpyruvic acid, ammonia, reduced NADH, and a proton.

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 and .

References