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. 2021 Apr 13;12:2195. doi: 10.1038/s41467-021-22504-6

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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. 2 — a Overlay of the active site of AnFDC with bound α-methyl cinnamic acid (dark green) from PDB:4ZA7, a model of ccMA (light green)-bound AnFDC with the lowest energy poses and a schematic design for ccMA. The negative hydrogen network and hydrophobic interactions are shown as dashed lines. b Relative decarboxylation activity of 25 AnFDC mutants designed for ccMA. The activity of WT AnFDC was defined as 1. The data are presented as the means ± SDs of three independent experiments (n = 3). c Simulated active site of the designed AnFDC Y394H:T395Q with bound ccMA. AnFDC ferulic acid decarboxylase derived from Aspergillus niger, mCA α-methyl cinnamic acid, ccMA cis,cis-muconic acid, SD standard deviation. Source data underlying Fig. 2b are provided as a Source Data file.