Ontology highlight
ABSTRACT:
SUBMITTER: Meng H
PROVIDER: S-EPMC4842997 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Meng Hengkai H Liu Pi P Sun Hongbing H Cai Zhen Z Zhou Jie J Lin Jianping J Li Yin Y
Scientific reports 20160425
Engineering the cofactor specificity of a natural enzyme often results in a significant decrease in its activity on original cofactor. Here we report that a NADH-dependent dehydrogenase (d-LDH) from Lactobacillus delbrueckii 11842 can be rationally engineered to efficiently use both NADH and NADPH as cofactors. Point mutations on three amino acids (D176S, I177R, F178T) predicted by computational analysis resulted in a modified enzyme designated as d-LDH*. The Kcat/Km of the purified d-LDH* on NA ...[more]