Homoserine dehydrogenase

In enzymology, a homoserine dehydrogenase is an enzyme that catalyzes the chemical reaction


 * L-homoserine + NAD(P)+ $$\rightleftharpoons$$ L-aspartate 4-semialdehyde + NAD(P)H + H+

The 3 substrates of this enzyme are L-homoserine, NAD+, and NADP+, whereas its 4 products are L-aspartate 4-semialdehyde, NADH, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-homoserine:NAD(P)+ oxidoreductase. Other names in common use include HSDH, and HSD. This enzyme participates in glycine, serine and threonine metabolism and lysine biosynthesis.

Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes, , , and.