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Kinetic Resolution of 4‐Hydroxy‐2‐ketones Catalyzed by a Baeyer–Villiger Monooxygenase
Author(s) -
Kirschner Anett,
Bornscheuer Uwe T.
Publication year - 2006
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.200602986
Subject(s) - kinetic resolution , monooxygenase , chemistry , catalysis , enantiomer , enantiomeric excess , resolution (logic) , biocatalysis , enzyme catalysis , enzyme , optically active , organic chemistry , stereochemistry , combinatorial chemistry , reaction mechanism , enantioselective synthesis , cytochrome p450 , artificial intelligence , computer science
Two with one stroke : The kinetic resolution of racemic 4‐hydroxy‐2‐ketones catalyzed by Baeyer–Villiger monooxygenase (BVMO) afforded not only the unreacted enantiomer in good optical purity but also allows access to optically active 1,2‐diols (see scheme). Thus, this enzymatic approach provides a range of products in a single reaction accessible otherwise only from reactions with ketoreductases and hydrolases.