In enzymology, a leucine dehydrogenase (EC 126.96.36.199) 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. This enzyme participates in valine, leucine and isoleucine degradation and valine, leucine and isoleucine biosynthesis.
LeuDH, Native (Bacillus cereus)
Enzyme Commission Number
60-120 units/mg protein (Lowry)
One unit will convert 1.0 μmole of L‑leucine to α-ketoisecaproate per min at pH 10.5 at 37°C.
leucine dehydrogenase; L-leucine dehydrogenase; L-leucine:NAD+ oxidoreductase (deaminating); LeuDH; EC 188.8.131.52; 9082-71-7