Carving the Active Site of Almond R-HNL for Increased Enantioselectivity

Structure‐guided redesign of the active site of almond (R)‐PaHNL5 for increased enantioselectivity resulted in four improved muteins. In particular, mutation V360I gave enhanced conversion rates and enantioselectivities higher than 96 % ee for two structurally related substrates 1 and 2. Chiral buil...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2005-07, Vol.44 (30), p.4700-4704
Main Authors: Weis, Roland, Gaisberger, Richard, Skranc, Wolfgang, Gruber, Karl, Glieder, Anton
Format: Article
Language:English
Subjects:
ACE inhibitors
Aldehyde-Lyases - chemistry
asymmetric synthesis
Binding Sites
biocatalysis
Catalysis
hydroxynitrile lyase
Isoenzymes - chemistry
Models, Molecular
Molecular Conformation
Nitriles - chemical synthesis
Nitriles - chemistry
protein engineering
Prunus - enzymology
Recombinant Proteins - chemistry
Stereoisomerism
Structure-Activity Relationship
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Summary:Structure‐guided redesign of the active site of almond (R)‐PaHNL5 for increased enantioselectivity resulted in four improved muteins. In particular, mutation V360I gave enhanced conversion rates and enantioselectivities higher than 96 % ee for two structurally related substrates 1 and 2. Chiral building blocks for the synthesis of pharmaceutically active “prils” (example shown) can thus be produced on a large scale.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200500435