Leucine Dehydrogenase

In enzymology, a leucine dehydrogenase (EC 1.4.1.9) 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.