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Determination of absolute configuration of secondary alcohols using lipase‐catalyzed kinetic resolutions
Author(s) -
Jing Qing,
Kazlauskas Romas J.
Publication year - 2008
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20543
Subject(s) - chemistry , kinetic resolution , lipase , absolute configuration , enantiomer , chirality (physics) , catalysis , kinetic energy , alcohol , computational chemistry , solvent , stereochemistry , organic chemistry , enantioselective synthesis , enzyme , physics , quantum mechanics , nambu–jona lasinio model , chiral symmetry breaking , quark
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 ∼50 secondary alcohols either as the only method or in combination with other methods. Chirality, 2008. © 2008 Wiley‐Liss, Inc.