2024-03-29T14:16:19Zhttps://eprints.lib.hokudai.ac.jp/dspace-oai/requestoai:eprints.lib.hokudai.ac.jp:2115/862752022-11-17T02:08:08Zhdl_2115_20044hdl_2115_124Argicyclamides A-C Unveil Enzymatic Basis for Guanidine Bis-prenylationPhan, Chin-Soon1000050812301Matsuda, KenichiBalloo, NandaniFujita, Kei1000070363900Wakimoto, Toshiyuki1000030280910Okino, Tatsufumiopen accessThis 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-VPFBI4B9YGSJDXAZUSAW430Guanidine 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.American Chemical Society2021-07-14engjournal articleAMhttp://hdl.handle.net/2115/86275https://doi.org/10.1021/jacs.1c057320002-7863AA00692602Journal of the American Chemical Society143271008310087https://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/86275/1/J.Am.Chem.Soc.143%2827%292021.pdfapplication/pdf360.64 KB2021-07-14https://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/86275/2/ja1c05732_si_001.pdfapplication/pdf6.97 MB2021-07-14