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A Tailor‐Made Chimeric Thiamine Diphosphate Dependent Enzyme for the Direct Asymmetric Synthesis of ( S )‐Benzoins
Author(s) -
Westphal Robert,
Vogel Constantin,
Schmitz Carlo,
Pleiss Jürgen,
Müller Michael,
Pohl Martina,
Rother Dörte
Publication year - 2014
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.201405069
Subject(s) - enzyme , thiamine , chemistry , steric effects , enantiomer , stereochemistry , biocatalysis , enantiomeric excess , combinatorial chemistry , biochemistry , catalysis , enantioselective synthesis , reaction mechanism
Thiamine diphosphate dependent enzymes are well known for catalyzing the asymmetric synthesis of chiral α‐hydroxy ketones from simple prochiral substrates. The steric and chemical properties of the enzyme active site define the product spectrum. Enzymes catalyzing the carboligation of aromatic aldehydes to ( S )‐benzoins have not so far been identified. We were able to close this gap by constructing a chimeric enzyme, which catalyzes the synthesis of various ( S )‐benzoins with excellent enantiomeric excess (>99 %) and very good conversion.