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Issue 22, 2015
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Hydrolase-catalyzed asymmetric carbon–carbon bond formation in organic synthesis

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Abstract

Enzyme catalytic promiscuity, in which the active site of an enzyme has the ability to catalyze more than one chemical transformation, has received widespread attention as more catalytic promiscuities of existing enzymes have been discovered. In this field, hydrolases have been mainly studied due to their commercial availability, high stability, broad substrate scope and high catalytic efficiency in media containing organic solvents. In this study, we review the hydrolase-catalyzed asymmetric carbon–carbon bond-forming reactions for the preparation of enantiomerically enriched compounds in organic synthesis. To date, these hydrolase-catalyzed asymmetric reactions include the direct asymmetric aldol, Michael, Mannich and Morita–Baylis–Hillman reactions. The hydrolase-catalyzed non-enantioselective examples were not included.

Graphical abstract: Hydrolase-catalyzed asymmetric carbon–carbon bond formation in organic synthesis

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Publication details

The article was received on 29 Sep 2014, accepted on 15 Jan 2015 and first published on 15 Jan 2015


Article type: Review Article
DOI: 10.1039/C4RA11462K
Citation: RSC Adv., 2015,5, 16801-16814
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    Hydrolase-catalyzed asymmetric carbon–carbon bond formation in organic synthesis

    Z. Guan, L. Li and Y. He, RSC Adv., 2015, 5, 16801
    DOI: 10.1039/C4RA11462K

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