This work was supported by the Swedish Research Council and the Erasmus program. The graphical material presenting the active sites of the lipases was prepared by Linda Fransson.
An S-Selective Lipase Was Created by Rational Redesign and the Enantioselectivity Increased with Temperature†
Article first published online: 23 JUN 2005
Copyright © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 44, Issue 29, pages 4582–4585, July 18, 2005
How to Cite
Magnusson, A. O., Takwa, M., Hamberg, A. and Hult, K. (2005), An S-Selective Lipase Was Created by Rational Redesign and the Enantioselectivity Increased with Temperature. Angew. Chem. Int. Ed., 44: 4582–4585. doi: 10.1002/anie.200500971
- Issue published online: 8 JUL 2005
- Article first published online: 23 JUN 2005
- Manuscript Received: 16 MAR 2005
- enzyme catalysis;
- protein engineering;
Higher activity with larger pockets: The figure shows a superposition of intermediates that occur in acyl transfer to (S)-1-phenylethanol catalyzed by Candida antarctica lipase B (CALB). Wild-type CALB cannot accomodate the phenyl group (gray) in the stereospecificity pocket and form all of the catalytically essential H bonds. The Trp 104 Ala mutation liberates the volume in yellow, the S enantiomer is easily fitted, and the specificity constant increases by a factor of 130 000.