Key points are not available for this paper at this time.
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.
Bartsch et al. (Fri,) studied this question.