title: Determination of absolute configuration of secondary alcohols using lipase-catalyzed kinetic resolutions.
abstract: Lipases show high enantioselectivity toward a wide range of secondary alcohols. An empirical rule based on the relative sizes of the substituents predicts which enantiomer reacts faster. X-ray structures of lipases provide a molecular basis for this empirical rule: their alcohol-binding pocket contains large hydrophobic pocket open to solvent and another smaller pocket. This predictable enantiopreference of lipases allows the determination of the absolute configuration of secondary alcohols using lipase-catalyzed kinetic resolution. Researchers have used this relative method to determine the configuration of approximately 50 secondary alcohols either as the only method or in combination with other methods.
authors.affiliation: Department of Biochemistry, Molecular Biology, and Biophysics and the Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota 55106-6104, USA.
authors.forename: Qing
authors.initials: Q
authors.lastname: Jing
authors.forename: Romas J
authors.initials: RJ
authors.lastname: Kazlauskas
mesh_terms: D000438:Alcohols / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D016956:Burkholderia cepacia / Q000201:enzymology; D002175:Candida / Q000201:enzymology; D007700:Kinetics; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008968:Molecular Conformation; D013237:Stereoisomerism
chemical_list: D000438:Alcohols; D008049:Lipase