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dc.contributor.authorMunakata, Ryosuke
dc.contributor.authorTakemura, Tomoya
dc.contributor.authorTatsumi, Kanade
dc.contributor.authorMoriyoshi, Eiko
dc.contributor.authorYanagihara, Koki
dc.contributor.authorSugiyama, Akifumi
dc.contributor.authorSuzuki, Hideyuki
dc.contributor.authorSeki, Hikaru
dc.contributor.authorMuranaka, Toshiya
dc.contributor.authorKawano, Noriaki
dc.contributor.authorYoshimatsu, Kayo
dc.contributor.authorKawahara, Nobuo
dc.contributor.authorYamaura, Takao
dc.contributor.authorGrosjean, Jérémy
dc.contributor.authorBourgaud, Frédéric
dc.contributor.authorHehn, Alain
dc.contributor.authorYazaki, Kazufumi
dc.contributor.alternative棟方, 涼介
dc.contributor.alternative杉山, 暁史
dc.contributor.alternative矢﨑, 一史
dc.date.accessioned2019-10-25T00:08:10Z-
dc.date.available2019-10-25T00:08:10Z-
dc.date.issued2019-09-24
dc.identifier.issn2399-3642
dc.identifier.urihttp://hdl.handle.net/2433/244385-
dc.descriptionアルテピリンC合成酵素の発見とその生産 --雑草の遺伝子から生理活性物質の生産へ--. 京都大学プレスリリース. 2019-10-25.
dc.description.abstractPlants produce various prenylated phenolic metabolites, including flavonoids, phloroglucinols, and coumarins, many of which have multiple prenyl moieties and display various biological activities. Prenylated phenylpropanes, such as artepillin C (3, 5-diprenyl-p-coumaric acid), exhibit a broad range of pharmaceutical effects. To date, however, no prenyltransferases (PTs) involved in the biosynthesis of phenylpropanes and no plant enzymes that introduce multiple prenyl residues to native substrates with different regio-specificities have been identified. This study describes the isolation from Artemisia capillaris of a phenylpropane-specific PT gene, AcPT1, belonging to UbiA superfamily. This gene encodes a membrane-bound enzyme, which accepts p-coumaric acid as its specific substrate and transfers two prenyl residues stepwise to yield artepillin C. These findings provide novel insights into the molecular evolution of this gene family, contributing to the chemical diversification of plant specialized metabolites. These results also enabled the design of a yeast platform for the synthetic biology of artepillin C.
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherSpringer Nature
dc.rights© The Author(s) 2019. 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/.
dc.titleIsolation of Artemisia capillaris membrane-bound di-prenyltransferase for phenylpropanoids and redesign of artepillin C in yeast
dc.type.niitypeJournal Article
dc.identifier.jtitleCommunications Biology
dc.identifier.volume2
dc.relation.doi10.1038/s42003-019-0630-0
dc.textversionpublisher
dc.identifier.artnum384
dc.identifier.kaken16H03282 / 17H05441
dc.relation.urlhttp://www.kyoto-u.ac.jp/ja/research/research_results/2019/191018_2.html
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