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Argicyclamides A-C Unveil Enzymatic Basis for Guanidine Bis-prenylation

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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
Type: article (author version)
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 脇本 敏幸

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