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. 2020 May 26;11:2644. doi: 10.1038/s41467-020-16341-2

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© The Author(s) 2020

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 View of the two enzymes (AHA in cyan and PPA in yellow)^36,38 with the bound substrate (blue carbons). The L7 loop partly covering the substrate is shown in purple for AHA and orange for PPA. b Close-up view of the active site with sidechains shown for AHA and the interactions between the nucleophile (Asp174) and general acid (Glu200) indicated with dashed lines (a crystallographically observed Cl⁻ ion is shown in green). c Optimized transition-state structure from DFT calculations of the model reaction in solution (atoms marked with asterisks were fixed).