An S‐Selective Lipase Was Created by Rational Redesign and the Enantioselectivity Increased with Temperature

Angewandte Chemie International EditionVolume 44, Issue 29 p. 4582-4585 Communication An S-Selective Lipase Was Created by Rational Redesign and the Enantioselectivity Increased with Temperature† Anders O. Magnusson, Anders O. Magnusson Royal Institute of Technology (KTH), Department of Biochemistry, School of Biotechnology, AlbaNova University Center, 106 91 Stockholm, Sweden, Fax: (+46) 8-5537-8468Search for more papers by this authorMohamad Takwa, Mohamad Takwa Royal Institute of Technology (KTH), Department of Biochemistry, School of Biotechnology, AlbaNova University Center, 106 91 Stockholm, Sweden, Fax: (+46) 8-5537-8468Search for more papers by this authorAnders Hamberg, Anders Hamberg Royal Institute of Technology (KTH), Department of Biochemistry, School of Biotechnology, AlbaNova University Center, 106 91 Stockholm, Sweden, Fax: (+46) 8-5537-8468Search for more papers by this authorKarl Hult Prof., Karl Hult Prof. kalle@biotech.kth.se Royal Institute of Technology (KTH), Department of Biochemistry, School of Biotechnology, AlbaNova University Center, 106 91 Stockholm, Sweden, Fax: (+46) 8-5537-8468Search for more papers by this author Anders O. Magnusson, Anders O. Magnusson Royal Institute of Technology (KTH), Department of Biochemistry, School of Biotechnology, AlbaNova University Center, 106 91 Stockholm, Sweden, Fax: (+46) 8-5537-8468Search for more papers by this authorMohamad Takwa, Mohamad Takwa Royal Institute of Technology (KTH), Department of Biochemistry, School of Biotechnology, AlbaNova University Center, 106 91 Stockholm, Sweden, Fax: (+46) 8-5537-8468Search for more papers by this authorAnders Hamberg, Anders Hamberg Royal Institute of Technology (KTH), Department of Biochemistry, School of Biotechnology, AlbaNova University Center, 106 91 Stockholm, Sweden, Fax: (+46) 8-5537-8468Search for more papers by this authorKarl Hult Prof., Karl Hult Prof. kalle@biotech.kth.se Royal Institute of Technology (KTH), Department of Biochemistry, School of Biotechnology, AlbaNova University Center, 106 91 Stockholm, Sweden, Fax: (+46) 8-5537-8468Search for more papers by this author First published: 08 July 2005 https://doi.org/10.1002/anie.200500971Citations: 110 † 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. Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract 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. Citing Literature Supporting Information Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2005/z500971_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article. Volume44, Issue29July 18, 2005Pages 4582-4585 RelatedInformation