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. 2023 Jul 24;14:4448. doi: 10.1038/s41467-023-40242-9

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© The Author(s) 2023

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 — Module I (coumaric acid biosynthesis module) includes modifications to boost intracellular tyrosine flux, as well as heterologous expression for efficient conversion of L-tyrosine to p-coumaric acid. Module II (ferulic acid biosynthesis module) incorporates heterologous enzymes with high efficiency for conversion of hydroxycinnamic acid substrates to ferulic acid in bacteria. Module III (eugenol biosynthesis module) includes heterologous enzymes for conversion of hydroxycinnamic acid substrates to phenylpropenes with high efficiency. Heterologous enzymes: fjTAL, tyrosine ammonia lyase from F. johnsoniae; seC3H, p-coumarate-3-hydroxylase from S. espanaensis; atCOMT, caffeic acid-o-methyltransferase from A. thaliana; at4CL1, 4-coumarate-CoA ligase from A. thaliana; llCCR, cinnamoyl-CoA reductase from L. leucocephala; scADH6, alcohol dehydrogenase 6 from S. cerevisiae; phCFAT, coniferyl alcohol acyltransferase from P. hybrida; phEGS, eugenol synthase from P. hybrida.