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. 2021 Jun 25;12:3983. doi: 10.1038/s41467-021-24259-6

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a Proposed mechanism of CvFAP-catalyzed decarboxylative deuteration. b Design of divergent directed evolution of CvFAP toward various substrates. c Docking result with nonanoic acid (green) and selected hot positions for protein engineering (PDB:5NCC)⁴⁹, FAD (flavin adenine dinucleotide) and some representative residues located at the entrance of the substrate pocket (yellow), binding region (orange) and reaction region (cyan) are represented by sticks with different colors. d The influence of kinetic isotope effect on the reaction activity. e The comparison of yields and TOF between WT-CvFAP and the best mutant (I398L) for the medium chain acid. f The comparison of yields and TOF between WT-CvFAP and the best mutant (G462A) for the short chain acid. g The enantiodivergent decarboxylative deuteration catalyzed by I398R and G462F mutants, respectively. h The comparison of yields and TOF between WT-CvFAP and the best mutant (Y466A) for bulky cyclic acid. Error bars represent the mean ± SD of three independent experiments. Source data are provided as a Source Data file.