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

Magnusson Anders O. | Zendy; Takwa Mohamad | Zendy; Hamberg Anders | Zendy; Hult Karl | Zendy

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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.

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