Structural and Biochemical Analyses of the Butanol Dehydrogenase from Fusobacterium nucleatum.

ABSTRACT: Butanol dehydrogenase (BDH) plays a significant role in the biosynthesis of butanol in bacteria by catalyzing butanal conversion to butanol at the expense of the NAD(P)H cofactor. BDH is an attractive enzyme for industrial application in butanol production; however, its molecular function remains largely uncharacterized. In this study, we found that Fusobacterium nucleatum YqdH (FnYqdH) converts aldehyde into alcohol by utilizing NAD(P)H, with broad substrate specificity toward aldehydes but not alcohols. An in vitro metal ion substitution experiment showed that FnYqdH has higher enzyme activity in the presence of Co²⁺. Crystal structures of FnYqdH, in its apo and complexed forms (with NAD and Co²⁺), were determined at 1.98 and 2.72 Å resolution, respectively.

SUBMITTER: Bai X 

PROVIDER: S-EPMC9917632 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature