Bacillus subtilis Esterase (BS2) and its Double Mutant Have Different Selectivity in the Removal of Carboxyl Protecting Groups

An esterase from Bacillus subtilis (BS2) and its double mutant E188W/M193C quickly hydrolyze n‐butyl, n‐propyl, methoxyethyl and allyl esters. The wild‐type BS2 preferentially removes such esters from the γ‐position of glutamate diesters, while the engineered enzyme has a reversed selectivity removing esters from the α‐position of glutamate diesters. Automated docking and molecular dynamic simulations were performed to understand the molecular reason for the different regioselectivity.