Molecular and Enzymatic Features of Homoserine Dehydrogenase from Bacillus subtilis.

ABSTRACT: Homoserine dehydrogenase (HSD) catalyzes the reversible conversion of _L-aspartate-4- semialdehyde to _L-homoserine in the aspartate pathway for the biosynthesis of lysine, methionine, threonine, and isoleucine. HSD has attracted great attention for medical and industrial purposes due to its recognized application in the development of pesticides and is being utilized in the large scale production of _L-lysine. In this study, HSD from Bacillus subtilis (BsHSD) was overexpressed in Escherichia coli and purified to homogeneity for biochemical characterization. We examined the enzymatic activity of BsHSD for _L-homoserine oxidation and found that BsHSD exclusively prefers NADP⁺ to NAD⁺ and that its activity was maxima

SUBMITTER: Kim DH 

PROVIDER: S-EPMC9728202 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature