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Complete Inversion of Enantioselectivity towards Acetylated Tertiary Alcohols by a Double Mutant of a Bacillus Subtilis Esterase
Author(s) -
Bartsch Sebastian,
Kourist Robert,
Bornscheuer Uwe T.
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200704606
Subject(s) - saturated mutagenesis , esterase , mutant , kinetic resolution , enzyme , chemistry , acetylation , mutagenesis , inversion (geology) , kinetic energy , substrate (aquarium) , amino acid , stereochemistry , biochemistry , biology , catalysis , enantioselective synthesis , physics , ecology , gene , paleontology , structural basin , quantum mechanics
Simultaneous saturation mutagenesis at three amino acid residues of esterase BS2 followed by high‐throughput screening identified a double mutant (E188W/M193C) with inverted enantiopreference, high E values, and broadened substrate range compared to the wild‐type (WT) enzyme, while the single mutants lacked this property. The kinetic resolution of ester 1 with the enzymes is shown in the scheme.