{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Guo S"],"funding":["National Science Foundation of China | National Natural Science Foundation of China-Yunnan Joint Fund"],"pagination":["2361"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9055067"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Darobactin is a ribosomally synthesized and post-translationally modified peptide (RiPP), which possesses potent activity against various Gram-negative bacteria. Darobactin features a highly unique bicyclic scaffold, consisting of an ether crosslink between two Trp residues and a C-C crosslink between a Lys and a Trp. Here we report in vivo and in vitro activity of darobactin synthase DarE. We show DarE is a radical S-adenosylmethionine (rSAM) enzyme and is solely responsible for forming the bicyclic scaffold of darobactin. DarE mainly produced the ether-crosslinked product in vitro, and when the assay was performed in H<sub>2</sub><sup>18</sup>O, apparent <sup>18</sup>O incorporation was observed into the ether-crosslinked product. These observations suggested an rSAM-dependent process in"],"journal":["Nature communications"],"pubmed_title":["Radical SAM-dependent ether crosslink in daropeptide biosynthesis."],"pmcid":["PMC9055067"],"funding_grant_id":["2018Y F A0900402"],"pubmed_authors":["Ding W","Ma S","Wang S","Deng Z","Guo S","Zhang Q"],"additional_accession":[]},"is_claimable":false,"name":"Radical SAM-dependent ether crosslink in daropeptide biosynthesis.","description":"Darobactin is a ribosomally synthesized and post-translationally modified peptide (RiPP), which possesses potent activity against various Gram-negative bacteria. Darobactin features a highly unique bicyclic scaffold, consisting of an ether crosslink between two Trp residues and a C-C crosslink between a Lys and a Trp. Here we report in vivo and in vitro activity of darobactin synthase DarE. We show DarE is a radical S-adenosylmethionine (rSAM) enzyme and is solely responsible for forming the bicyclic scaffold of darobactin. DarE mainly produced the ether-crosslinked product in vitro, and when the assay was performed in H<sub>2</sub><sup>18</sup>O, apparent <sup>18</sup>O incorporation was observed into the ether-crosslinked product. These observations suggested an rSAM-dependent process in","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2025-04-05T13:23:25.844Z","creation":"2025-04-05T13:23:25.844Z"},"accession":"S-EPMC9055067","cross_references":{"pubmed":["35487921"],"doi":["10.1038/s41467-022-30084-2"]}}