An S‐Selective Lipase Was Created by Rational Redesign and the Enantioselectivity Increased with Temperature
- 8 July 2005
- journal article
- research article
- Published by Wiley in Angewandte Chemie International Edition in English
- Vol. 44 (29) , 4582-4585
- https://doi.org/10.1002/anie.200500971
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Creating Space for Large Secondary Alcohols by Rational Redesign of Candida antarctica Lipase BChemBioChem, 2005
- Highly Compatible Metal and Enzyme Catalysts for Efficient Dynamic Kinetic Resolution of Alcohols at Ambient TemperatureAngewandte Chemie, 2004
- Highly Compatible Metal and Enzyme Catalysts for Efficient Dynamic Kinetic Resolution of Alcohols at Ambient TemperatureAngewandte Chemie International Edition in English, 2004
- (S)-Selective Dynamic Kinetic Resolution of Secondary Alcohols by the Combination of Subtilisin and an Aminocyclopentadienylruthenium Complex as the CatalystsJournal of the American Chemical Society, 2003
- Substrate entropy in enzyme enantioselectivity: An experimental and molecular modeling study of a lipaseProtein Science, 2002
- Complete reversal of enantioselectivity of an enzyme-catalyzed reaction by directed evolutionChemical Communications, 2001
- The Temperature Dependence of Enzymatic Kinetic Resolutions Reveals the Relative Contribution of Enthalpy and Entropy to Enzymatic EnantioselectivityBiocatalysis and Biotransformation, 1999
- Temperature effects on S1- and S1′-enantioselectivity of α-chymotrypsinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
- Temperature modulation of the stereochemistry of enzymatic catalysis: Prospects for exploitationTrends in Biotechnology, 1996
- Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcoholsBiochemistry, 1995