L-erythro-3,5-diaminohexanoate dehydrogenase

In enzymology, a L-erythro-3,5-diaminohexanoate dehydrogenase is an enzyme that catalyzes the chemical reaction


 * L-erythro-3,5-diaminohexanoate + H2O + NAD+ $$\rightleftharpoons$$ (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+

The 3 substrates of this enzyme are L-erythro-3,5-diaminohexanoate, H2O, and NAD+, whereas its 4 products are (S)-5-amino-3-oxohexanoate, 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-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating). This enzyme is also called L-3,5-diaminohexanoate dehydrogenase. This enzyme participates in lysine degradation.