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. 2022 Dec 9;13:7624. doi: 10.1038/s41467-022-33576-3

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© The Author(s) 2022

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. 3 — a Key reactions catalyzed by E. lenta catechol dehydroxylases. b Genomic contexts of dadh in the non-dopamine metabolizing strain E. lenta DSM 2243 and the dopamine-metabolizing E. lenta A2. c Genomic contexts of cadh and hcdh in E. lenta DSM 2243. d Design of P_dadh reporters pXD70LacZ2 and pXD70LacZ7, P_cadh reporters pXD70LacZ8.1 and pXD70LacZ8, and P_hcdh reporters pXD70LacZ9 and pXD70LacZ9.1. e LacZ assays revealed the transcriptional response of catechol dehydroxylase promoter reporters to corresponding catechols. f LacZ assays revealed the high specificity of each catechol dehydroxylase promoter construct for individual enzyme substrates. Data represented as mean ± SD with n = 3 biological replicates for e and f. Source data are provided as a Source Data file.