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An S ‐Selective Lipase Was Created by Rational Redesign and the Enantioselectivity Increased with Temperature
Author(s) -
Magnusson Anders O.,
Takwa Mohamad,
Hamberg Anders,
Hult Karl
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200500971
Subject(s) - candida antarctica , stereospecificity , enantiomer , lipase , chemistry , stereochemistry , catalysis , enzyme , organic chemistry
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.