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Abstract Ketoreductase ChKRED12 from Chryseobacterium sp. CA49 was identified as a highly stereoselective catalyst for the bioreductive production of (2S,3S)-ethyl 3-hydroxy-2-methoxy-3-phenylpropanoate (EMHP) through dynamic kinetic resolution. Its performance was further… Click to show full abstract
Abstract Ketoreductase ChKRED12 from Chryseobacterium sp. CA49 was identified as a highly stereoselective catalyst for the bioreductive production of (2S,3S)-ethyl 3-hydroxy-2-methoxy-3-phenylpropanoate (EMHP) through dynamic kinetic resolution. Its performance was further improved using semi-rational design strategies targeting residues Gln151 and Met191. Mutant M191S displayed enhanced activity (4-fold), producing (2S,3S)-EMHP with >99% ee and > 99/1 dr; two double mutants (Q151F/M191 L and Q151Y/M191 L) displayed reversed stereoselectivity and enhanced activity (~3-fold), producing (2R,3R)-EMHP with >99% ee and 98/2 dr. Models of the mutants docked with the substrate and NAD+ revealed possible mechanism of the improved characteristics.
Journal Title: Catalysis Communications
Year Published: 2020
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