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