Expanding the Catalytic Triad in Epoxide Hydrolases and Related Enzymes.

ABSTRACT: Potato epoxide hydrolase 1 exhibits rich enantio- and regioselectivity in the hydrolysis of a broad range of substrates. The enzyme can be engineered to increase the yield of optically pure products as a result of changes in both enantio- and regioselectivity. It is thus highly attractive in biocatalysis, particularly for the generation of enantiopure fine chemicals and pharmaceuticals. The present work aims to establish the principles underlying the activity and selectivity of the enzyme through a combined computational, structural, and kinetic study using the substrate trans-stilbene oxide as a model system. Extensive empirical valence bond simulations have been performed on the wild-type enzyme together with several experimentally characterized mutants. We are able to computation

SUBMITTER: Amrein BA 

PROVIDER: S-EPMC4613740 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature