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

Bornscheuer, Uwe T., Kazlauskas, Romas J.·2004·Angewandte Chemie International Edition

Abstract

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.

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Metadata

Authors
Bornscheuer, U. T., & Kazlauskas, R. J.
Venue
Angewandte Chemie International Edition
Publisher
Wiley
Published
2004-11-17
Volume
43
Issue
45
Pages
6032-6040
ISSN
  • 1433-7851 (ISSN-L)
  • 1521-3773
OpenAlex
W2110198171
Cited by
603
References
0
FWCI
8.97
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Catalytic Promiscuity in Biocatalysis: Using Old Enzymes to Form New Bonds and Follow New Pathways. https://app.cochat.ai/papers/10.1002/anie.200460416
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Bornscheuer, U. T., & Kazlauskas, R. J. (2004). Catalytic Promiscuity in Biocatalysis: Using Old Enzymes to Form New Bonds and Follow New Pathways. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.200460416

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.