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Issue 12, 2013
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Benzaldehyde lyase-catalyzed diastereoselective C–C bond formation by simultaneous carboligation and kinetic resolution

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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.

Graphical abstract: Benzaldehyde lyase-catalyzed diastereoselective C–C bond formation by simultaneous carboligation and kinetic resolution

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Supplementary files

Article information


Submitted
10 May 2012
Accepted
06 Dec 2012
First published
06 Dec 2012

Org. Biomol. Chem., 2013,11, 2000-2004
Article type
Paper

Benzaldehyde lyase-catalyzed diastereoselective C–C bond formation by simultaneous carboligation and kinetic resolution

C. R. Müller, M. Pérez-Sánchez and P. Domínguez de María, Org. Biomol. Chem., 2013, 11, 2000
DOI: 10.1039/C2OB27344F

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