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.
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Bartsch et al. (2008) studied this question.
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