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• W2010116257 abstract "Enzymes create chiral microenvironments that may simultaneously generate several stereogenic centers in the same catalytic cycle, broadening the possibilities of biocatalysis. Benzaldehyde lyase (BAL) affords highly diastereoselective α-hydroxy-ketones by simultaneously performing ligation and kinetic resolution of a racemic aldehyde. Thus, to the well-known enantioselective BAL-carboligation of aldehydes (C–C bond formation), another property, namely diastereoselectivity, is added in this paper for the first time." @default.
• W2010116257 created "2016-06-24" @default.
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• W2010116257 date "2013-01-01" @default.
• W2010116257 modified "2023-10-01" @default.
• W2010116257 title "Benzaldehyde lyase-catalyzed diastereoselective C–C bond formation by simultaneous carboligation and kinetic resolution" @default.
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• W2010116257 doi "https://doi.org/10.1039/c2ob27344f" @default.
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