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Phenylalanine dehydrogenase : ウィキペディア英語版 | Phenylalanine dehydrogenase
In enzymology, a phenylalanine dehydrogenase () 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==
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
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