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Argicyclamides A-C Unveil Enzymatic Basis for Guanidine Bis-prenylation
| Title: | Argicyclamides A-C Unveil Enzymatic Basis for Guanidine Bis-prenylation |
| Authors: | Phan, Chin-Soon Browse this author | | Matsuda, Kenichi Browse this author →KAKEN DB | | Balloo, Nandani Browse this author | | Fujita, Kei Browse this author | | Wakimoto, Toshiyuki Browse this author →KAKEN DB | | Okino, Tatsufumi Browse this author →KAKEN DB |
| Issue Date: | 14-Jul-2021 |
| Publisher: | American Chemical Society |
| Journal Title: | Journal of the American Chemical Society |
| Volume: | 143 |
| Issue: | 27 |
| Start Page: | 10083 |
| End Page: | 10087 |
| Publisher DOI: | 10.1021/jacs.1c05732 |
| Abstract: | Guanidine prenylation is an outstanding modification in alkaloid and peptide biosynthesis, but its enzymatic basis has remained elusive. We report the isolation of argicyclamides, a new class of cyanobactins with unique mono- and bis-prenylations on guanidine moieties, from Microcystis aeruginosa NIES-88. The genetic basis of argicyclamide biosynthesis was established by the heterologous expression and in vitro characterization of biosynthetic enzymes including AgcF, a new guanidine prenyltransferase. This study provides important insight into the biosynthesis of prenylated guanidines and offers a new toolkit for peptide modification. |
| Rights: | This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/articlesonrequest/AOR-VPFBI4B9YGSJDXAZUSAW |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/86275 |
| Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 脇本 敏幸
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