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
experimental part
p. 2325 - 2332
(2009/12/28)
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