title: Benzaldehyde lyase-catalyzed diastereoselective C-C bond formation by simultaneous carboligation and kinetic resolution.
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.
authors.affiliation: Institut für Technische und Makromolekulare Chemie (ITMC), RWTH Aachen University, Worringerweg 1, 52074 Aachen, Germany.
authors.forename: Christoph R
authors.initials: CR
authors.lastname: Müller
authors.forename: María
authors.initials: M
authors.lastname: Pérez-Sánchez
authors.forename: Pablo
authors.initials: P
authors.lastname: Domínguez de María
mesh_terms: D000446:Aldehyde-Lyases / Q000737:chemistry / Q000378:metabolism*; D000447:Aldehydes / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D007659:Ketones / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D015394:Molecular Structure; D013237:Stereoisomerism
chemical_list: D000447:Aldehydes; D007659:Ketones; D000446:Aldehyde-Lyases; C059416:benzaldehyde lyase