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New additions to the arsenal of biocatalysts for noncanonical amino acid synthesis

Alfonzo, Edwin and Das, Anuvab and Arnold, Frances H. (2022) New additions to the arsenal of biocatalysts for noncanonical amino acid synthesis. Current Opinion in Green and Sustainable Chemistry, 38 . Art. No. 100701. ISSN 2452-2236. doi:10.1016/j.cogsc.2022.100701.

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Noncanonical amino acids (ncAAs) merge the conformational behavior and native interactions of proteinogenic amino acids with nonnative chemical motifs and have proven invaluable in developing modern therapeutics. This blending of native and nonnative characteristics has resulted in essential drugs like nirmatrelvir, which comprises three ncAAs and is used to treat COVID-19. Enzymes are appearing prominently in recent syntheses of ncAAs, where they demonstrate impressive control over the stereocenters and functional groups found therein. Here we review recent efforts to expand the biocatalyst arsenal for synthesizing ncAAs with natural enzymes. We also discuss how new-to-nature enzymes can contribute to this effort by catalyzing reactions inspired by the vast repertoire of chemical catalysis and acting on substrates that would otherwise not be used in synthesizing ncAAs. Abiotic enzyme-catalyzed reactions exploit the selectivity afforded by a macromolecular catalyst to access molecules not available to natural enzymes and perhaps not even chemical catalysis.

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URLURL TypeDescription
Alfonzo, Edwin0000-0002-4112-8751
Das, Anuvab0000-0002-9344-4414
Arnold, Frances H.0000-0002-4027-364X
Additional Information:This work was supported by the National Institute of General Medical Sciences (grant R01GM125887). E.A. was supported by a Ruth Kirschstein NIH Postdoctoral Fellowship (F32GM143799). The authors thank Dr. Sabine Brinkmann-Chen and Dr. Zhen Liu for assistance in preparing this manuscript.
Funding AgencyGrant Number
NIH Postdoctoral FellowshipF32GM143799
Record Number:CaltechAUTHORS:20221128-494241100.12
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:118056
Deposited By: Research Services Depository
Deposited On:11 Dec 2022 20:56
Last Modified:13 Dec 2022 17:47

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