An S-selective lipase was created by rational redesign and the enantioselectivity increased with temperature

• 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.

Nyckelord

enantioselectivity

enzyme catalysis

hydrolases

protein engineering

thermodynamics

DYNAMIC KINETIC RESOLUTION

SECONDARY ALCOHOLS

STEREOSELECTIVITY

STEREOCHEMISTRY

RECOGNITION

ENANTIOMERS

CATALYSTS

ENTROPY

CEPACIA

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