Journal
ADVANCED SYNTHESIS & CATALYSIS
Volume 351, Issue 4, Pages 583-588Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/adsc.200900045
Keywords
bioreduction; diaryl ketones; enantioselectivity; enzyme catalysis; oxidoreductase
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Funding
- Chinese Academy of Sciences [KSCX2-YW-G-031]
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The carbonyl reductase from red yeast Sporobolomyces salmonicolor AKU4429 (SSCR) and its mutant enzymes effectively catalyzed the enantioselective reduction of diaryl ketones to give the corresponding chiral alcohols. Both conversion and enantioselectivity were dependent on the co-solvent in the reaction medium. Diaryl ketones with a para-substituent on one of the phenyl groups were reduced with high enantioselectivity (up to 99% ee), which is difficult to achieve using chemical methods such as chiral borane reduction, asymmetric hydrogenation or hydrosilylation. Mutation of SSCR at Q245 resulted in a higher amount of (S)-enantiomer in the products, and in the case of mutant Q245P with para-substituted diaryl ketones as substrate, this effect was so remarkable that the reduction enantio-preference was switched from (R) to (S). The present study provides valuable information about the catalytic properties of the carbonyl reductase SSCR toward the reduction of diaryl ketones, serving as basis for further engineering of this enzyme to develop efficient biocatalysts for highly enantiospecific reduction of diaryl ketones without high electronic dissymmetry or an ortho-substituent on one of the aryl groups.
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