In enzymology, L-erythro-3,5-diaminohexanoate dehydrogenase () is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are L-erythro-3,5-diaminohexanoic acid, water, and oxidised nicotinamide adenine dinucleotide (NAD<sup>+</sup>). Its products are (S)-5-amino-3-oxohexanoic acid, reduced NADH, ammonia, and a proton.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH<sub>2</sub> group of donors with NAD<sup>+</sup> or NADP<sup>+</sup> 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.