Homoserine dehydrogenase (HSDH)

Homoserine dehydrogenase is an enzyme (EC 1.1.1.3) that catalyzes the reversible conversion of L-aspartate-4-semialdehyde to L-homoserine, the third step in the aspartate pathway, which is essential for the biosynthesis of several amino acids (threonine, methionine, isoleucine, and lysine) in bacteria, fungi, and plants[1][2][3][4][6][7]. It is a dimeric oxidoreductase containing nucleotide-binding and substrate-binding domains and, in some forms, a regulatory ACT domain[2]. Homoserine dehydrogenase is found as a monofunctional enzyme in some organisms or as part of a bifunctional aspartokinase-homoserine dehydrogenase in others[1]. As it is not present in humans, it has emerged as a potential therapeutic target for novel antifungal agents and for antimicrobial drug development against pathogens that utilize this biosynthetic route[4].

Other names

HSDHHSDL-homoserine:NAD(P)+ oxidoreductaseaspartate-semialdehyde reductase

Inhibitors block the NAD(P)-dependent reduction of aspartate-beta-semialdehyde to homoserine, interrupting essential amino acid biosynthesis in fungi and bacteria.