Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substratesThis article is part of the ‘Enzymes and Proteins’ web-theme issue for ChemComm.Electronic supplementary information (ESI) available: Site-directed mutagenesis, synthesis of 1, lipase-catalyzed kinetic resolution of 1, determination of kinetic constants, design of mutants, and copies of NMR spectra. See DOI: 10.1039/c001561j

Catalytic activity and enantioselectivity of lipase toward poor substrates bearing bulky substituents on both sides have been dramatically improved by rational design; the Evalue for a poor substrate was increased from 5 (wild-type enzyme) to >200 (I287F/I290A double mutant) with an acceleration of the reaction rate. [ABSTRACT FROM AUTHOR]