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Bacillus subtilis Esterase (BS2) and its Double Mutant Have Different Selectivity in the Removal of Carboxyl Protecting Groups
Author(s) -
Barbayianni Efrosini,
Kokotos Christoforos G.,
Bartsch Sebastian,
Drakou Christina,
Bornscheuer Uwe T.,
Kokotos George
Publication year - 2009
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200900325
Subject(s) - chemistry , bacillus subtilis , esterase , selectivity , regioselectivity , mutant , hydrolysis , enzyme , stereochemistry , combinatorial chemistry , organic chemistry , biochemistry , catalysis , gene , bacteria , genetics , biology
Abstract 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.