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Leucine dehydrogenase : ウィキペディア英語版 | Leucine dehydrogenase
In enzymology, a leucine dehydrogenase () is an enzyme that catalyzes the chemical reaction :L-leucine + H2O + NAD+ 4-methyl-2-oxopentanoate + NH3 + NADH + H+ The 3 substrates of this enzyme are L-leucine, H2O, and NAD+, whereas its 4 products are 4-methyl-2-oxopentanoate, 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-leucine:NAD+ oxidoreductase (deaminating). Other names in common use include L-leucine dehydrogenase, L-leucine:NAD+ oxidoreductase, deaminating, and LeuDH. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis. ==Structural studies==
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
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