Expanding the Catalytic Triad in Epoxide Hydrolases and Related Enzymes.

Amrein BA, Bauer P, Duarte F, Janfalk Carlsson Å, Naworyta A, Mowbray SL, Widersten M, Kamerlin SC

ACS Catal 5 (10) 5702-5713 [2015-10-02; online 2015-08-17]

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

Affiliated researcher

PubMed 26527505

DOI 10.1021/acscatal.5b01639

Crossref 10.1021/acscatal.5b01639

pmc: PMC4613740


Publications 7.2.9