Catalytic Promiscuity in Biocatalysis: Using Old Enzymes to Form New Bonds and Follow New Pathways

Biocatalysis has expanded rapidly in the last decades with the discoveries of highly stereoselective enzymes with broad substrate specificity. A new frontier for biocatalysis is broad reaction specificity, where enzymes catalyze alternate reactions. Although often underappreciated, catalytic promisc...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2004-11, Vol.43 (45), p.6032-6040
Main Authors: Bornscheuer, Uwe T., Kazlauskas, Romas J.
Format: Article
Language:English
Subjects:
biosynthesis
Biotechnology - methods
biotransformations
Catalysis
enzyme catalysis
Enzymes - chemistry
Enzymes - metabolism
molecular modeling
Molecular Structure
Protein Engineering
proteins
Proteins - chemistry
Proteins - metabolism
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Summary:Biocatalysis has expanded rapidly in the last decades with the discoveries of highly stereoselective enzymes with broad substrate specificity. A new frontier for biocatalysis is broad reaction specificity, where enzymes catalyze alternate reactions. Although often underappreciated, catalytic promiscuity has a natural role in evolution and occasionally in the biosynthesis of secondary metabolites. Examples of catalytic promiscuity with current or potential applications in synthesis are reviewed here. Combined with protein engineering, the catalytic promiscuity of enzymes may broadly extend their usefulness in organic synthesis. Unfaithful enzymes, that is, enzymes that catalyze alternative reactions, play a natural role in evolution and occasionally in the biosynthesis of secondary metabolites. In one example pyruvate decarboxylase catalyzes not only the natural reaction (A) but also the enantioselective acyloin condensation of acetaldehyde and benzaldehyde (B).
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200460416