An S-selective lipase was created by rational redesign and the enantioselectivity increased with temperature
2005 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 44, no 29, 4582-4585 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2005. Vol. 44, no 29, 4582-4585 p.
enantioselectivity, enzyme catalysis, hydrolases, protein engineering, thermodynamics, DYNAMIC KINETIC RESOLUTION, SECONDARY ALCOHOLS, STEREOSELECTIVITY, STEREOCHEMISTRY, RECOGNITION, ENANTIOMERS, CATALYSTS, ENTROPY, CEPACIA
IdentifiersURN: urn:nbn:se:kth:diva-13009DOI: 10.1002/anie.200500971ISI: 000230737500019ScopusID: 2-s2.0-22744445622OAI: oai:DiVA.org:kth-13009DiVA: diva2:320246