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Benzaldehyde lyase-catalyzed diastereoselective C-C bond formation by simultaneous carboligation and kinetic
Christoph R Müller1, María Pérez-Sánchez, Pablo Domínguez de María
1Institut für Technische und Makromolekulare Chemie (ITMC), RWTH Aachen University, Worringerweg 1, 52074 Aachen, Germany.
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.
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