Determination of absolute configuration of secondary alcohols using lipase-catalyzed kinetic resolutions.
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.
Jing
Qing
Q
Department of Biochemistry, Molecular Biology, and Biophysics and the Biotechnology Institute, University of Minnesota, Saint Paul, Minnesota 55106-6104, USA.
Kazlauskas
Romas J
RJ
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
D000438:Alcohols; D008049:Lipase