Engineering new catalytic activities in enzymes
- Creators
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Chen, Kai
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Arnold, Frances H.
Abstract
The efficiency, selectivity and sustainability benefits offered by enzymes are enticing chemists to consider biocatalytic transformations to complement or even supplant more traditional synthetic routes. Increasing demands for efficient and versatile synthetic methods, combined with powerful new discovery and engineering tools, has prompted innovations in biocatalysis, especially the development of new enzymes for precise transformations or 'molecular editing'. As a result, the past decade has witnessed an impressive expansion of the catalytic repertoire of enzymes to include new and useful transformations not known (or relevant) in the biological world. In this Review we illustrate various ways in which researchers have approached using the catalytic machineries of enzymes for new-to-nature transformations. These efforts have identified genetically encoded catalysts that can be tuned and diversified by engineering the protein sequence, particularly by directed evolution. Discovery and improvement of these new enzyme activities is opening a floodgate that connects the chemistry of the biological world to that invented by humans over the past 100 years.
Additional Information
© 2020 Springer Nature Limited. Received 25 August 2019; Accepted 21 October 2019; Published 20 January 2020. We thank D. J. Wackelin and Y. Yang (Caltech) for helpful discussions and comments on the manuscript. This work was supported by NSF Division of Molecular and Cellular Biosciences grant no. MCB-1513007, the US Army Research Office Institute for Collaborative Biotechnologies (cooperative agreement no. W911NF-19-2-0026) and the US Army Research Office Institute for Collaborative Biotechnologies (contract no. W911NF-19-D-0001). K.C. thanks the Resnick Sustainability Institute at Caltech for fellowship support. The content of this paper does not necessarily reflect the position or the policy of the funding agencies, and no official endorsement should be inferred. Author Contributions: All authors participated in designing and writing the manuscript. The authors declare no competing interests.Additional details
- Eprint ID
- 100816
- DOI
- 10.1038/s41929-019-0385-5
- Resolver ID
- CaltechAUTHORS:20200121-114421759
- NSF
- MCB-1513007
- Army Research Office (ARO)
- W911NF-19-2-0026
- Army Research Office (ARO)
- W911NF-19-D-0001
- Resnick Sustainability Institute
- Created
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2020-01-21Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field
- Caltech groups
- Resnick Sustainability Institute, Division of Biology and Biological Engineering