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Combining chemistry and protein engineering for new-to-nature biocatalysis

Miller, David C. and Athavale, Soumitra V. and Arnold, Frances H. (2022) Combining chemistry and protein engineering for new-to-nature biocatalysis. Nature Synthesis, 1 (1). pp. 18-23. ISSN 2731-0582. PMCID PMC8995090. doi:10.1038/s44160-021-00008-x. https://resolver.caltech.edu/CaltechAUTHORS:20220112-597412800

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Abstract

Biocatalysis, the application of enzymes to solve synthetic problems of human import, has blossomed into a powerful technology for chemical innovation. In the past decade, a threefold partnership, where nature provides blueprints for enzymatic catalysis, chemists introduce innovative activity modes with abiological substrates, and protein engineers develop new tools and algorithms to tune and improve enzymatic function, has unveiled the frontier of new-to-nature enzyme catalysis. In this Perspective, we highlight examples of interdisciplinary studies, which have helped to expand the scope of biocatalysis, including concepts of enzymatic versatility explored through the lens of biomimicry, to achieve activities and selectivities beyond those currently possible with chemocatalysis. We indicate how modern tools, such as directed evolution, computational protein design and machine learning-based protein engineering methods, have already impacted and will continue to influence enzyme engineering for new abiological transformations. A sustained collaborative effort across disciplines is anticipated to spur further advances in biocatalysis in the coming years.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1038/s44160-021-00008-xDOIArticle
https://rdcu.be/cLiabPublisherFree ReadCube access
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8995090PubMed CentralArticle
ORCID:
AuthorORCID
Miller, David C.0000-0002-4560-8824
Athavale, Soumitra V.0000-0001-5620-6997
Arnold, Frances H.0000-0002-4027-364X
Additional Information:© 2022 Nature Publishing Group. Received 08 October 2021; Accepted 15 November 2021; Published 12 January 2022. This report was prepared as an account of work sponsored by an agency of the United States Government. Neither the United States Government nor any agency thereof, nor any of their employees, makes any warranty, express or implied, or assumes any legal liability or responsibility for the accuracy, completeness, or usefulness of any information, apparatus, product, or process disclosed, or represents that its use would not infringe on privately owned rights. Reference herein to any specific commercial product, process, or service by trade name, trademark, manufacturer, or otherwise does not necessarily constitute or imply its endorsement, recommendation, or favouring by the United States Government or any agency thereof. The views and opinions of the authors expressed herein do not necessarily state or reflect those of the United States Government or any agency thereof. D.C.M. was supported by a Ruth Kirschstein NIH Postdoctoral Fellowship (F32GM128247). This work was sponsored by the US Army Research Office and accomplished under cooperative agreement W911NF-19-2-0026 for the Institute of Collaborative Biotechnologies. This material is based on work sponsored by the US Department of Energy, Office of Basic Energy Sciences, under award number DE-SC0021141. We wish to thank E. Alfonzo, R. Mao and K. E. Johnston for helpful discussions. All protein structures were prepared using PyMOL (The PyMOL Molecular Graphics System, v.2.0 Schrödinger, LLC). The authors declare no competing interests. Peer review information: Nature Synthesis thanks Gerard Roelfes and the other, anonymous, reviewer(s) for their contribution to the peer review of this work. Alison Stoddart was the primary editor on this article and managed its editorial process and peer review in collaboration with the rest of the editorial team.
Funders:
Funding AgencyGrant Number
NIH Postdoctoral FellowshipF32GM128247
Army Research Office (ARO)W911NF-19-0026
Department of Energy (DOE)DE-SC0021141
Subject Keywords:Biocatalysis; Synthetic chemistry methodology
Issue or Number:1
PubMed Central ID:PMC8995090
DOI:10.1038/s44160-021-00008-x
Record Number:CaltechAUTHORS:20220112-597412800
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20220112-597412800
Official Citation:Miller, D.C., Athavale, S.V. & Arnold, F.H. Combining chemistry and protein engineering for new-to-nature biocatalysis. Nat Synth 1, 18–23 (2022). https://doi.org/10.1038/s44160-021-00008-x
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:112850
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:12 Jan 2022 23:45
Last Modified:25 Jul 2022 17:59

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