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 y-position of glutamate diesters, while the engineered enzyme has a reversed selectivity removing esters from the a-position of glutamate diesters. Automated docking and molecular dynamic simulations were performed to understand the molecular reason for the different regioselectivity.
Barbayianni, Efrosini,Kokotos, Christoforos G.,Bartsch, Sebastian,Drakou, Christina,Bornscheuer, Uwe T.,Kokotos, George