{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Choi B"],"funding":["Princeton University","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["11605-11609"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11064158"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["146(17)"],"pubmed_abstract":["The ribosomally synthesized and post-translationally modified peptide (RiPP) superfamily of natural products includes many examples of cyclic peptides with diverse macrocyclization chemistries. The graspetides, one family of macrocyclized RiPPs, harbor side chain-side chain ester or amide linkages. We recently reported the structure and biosynthesis of the graspetide pre-fuscimiditide, a 22-amino-acid (aa) peptide with two ester cross-links forming a stem-loop structure. These cross-links are introduced by a single graspetide synthetase, the ATP-grasp enzyme ThfB. Here we show that ThfB can also catalyze the formation of amide or thioester cross-links in prefuscimiditide, with thioester formation being especially efficient. We further show that upon proteolysis to reveal an N-terminal cyst"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Cyclic Peptides from Graspetide Biosynthesis and Native Chemical Ligation."],"pmcid":["PMC11064158"],"funding_grant_id":["R01 GM107036","GM107036"],"pubmed_authors":["Choi B","Link AJ","Acuna A"],"additional_accession":[]},"is_claimable":false,"name":"Cyclic Peptides from Graspetide Biosynthesis and Native Chemical Ligation.","description":"The ribosomally synthesized and post-translationally modified peptide (RiPP) superfamily of natural products includes many examples of cyclic peptides with diverse macrocyclization chemistries. The graspetides, one family of macrocyclized RiPPs, harbor side chain-side chain ester or amide linkages. We recently reported the structure and biosynthesis of the graspetide pre-fuscimiditide, a 22-amino-acid (aa) peptide with two ester cross-links forming a stem-loop structure. These cross-links are introduced by a single graspetide synthetase, the ATP-grasp enzyme ThfB. Here we show that ThfB can also catalyze the formation of amide or thioester cross-links in prefuscimiditide, with thioester formation being especially efficient. We further show that upon proteolysis to reveal an N-terminal cyst","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-02T20:58:17.866Z","creation":"2025-06-25T03:06:22.194Z"},"accession":"S-EPMC11064158","cross_references":{"pubmed":["38634647"],"doi":["10.1021/jacs.4c02745"]}}