Structure-Guided Regulation in the Enantioselectivity of an Epoxide Hydrolase to Produce Enantiomeric Monosubstituted Epoxides and Vicinal Diols via Kinetic Resolution.

Structure-guided microtuning of an epoxide hydrolase was executed. One mutant, A214C/A250I, displayed a 12.6-fold enhanced enantiomeric ratio ( = 202) toward -styrene oxide, achieving its nearly perfect kinetic resolution at 0.8 M in pure water or 1.6 M in -hexanol/water. Several other beneficial mutants also displayed significantly improved values, offering promising biocatalysts to access 19 structurally diverse chiral monosubstituted epoxides (97.1 - ≥ 99% ee) and vicinal diols (56.2-98.0% ee) with high yields.