Exploration of the cofactor specificity of wild-type phosphite dehydrogenase and its mutant using molecular dynamics simulations.

ABSTRACT: Phosphite dehydrogenase (Pdh) catalyzes the NAD-dependent oxidation of phosphite to phosphate with the formation of NADH. It can be used in several bioorthogonal systems for metabolic control and related applications, for example, bioelectricity. At present, NAD has poor stability at high concentrations and costs are expensive. Implementation of a non-natural cofactor alternative to the ubiquitous redox cofactor nicotinamide adenosine dinucleotide (NAD) is of great scientific and biotechnological interest. Several Pdhs have been engineered to favor a smaller-sized NAD analogue with a cheaper price and better thermal stability, namely, nicotinamide cytosine dinucleotide (NCD). However, the conformational changes of two cofactors binding to Pdh remain unknown. In this study, five molecular d

SUBMITTER: Liu K 

PROVIDER: S-EPMC8697927 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature