{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sarksian R"],"funding":["National Center for Research Resources","NCRR NIH HHS","Howard Hughes Medical Institute","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["2551-2558"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9486935"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(9)"],"pubmed_abstract":["The three-dimensional structure of natural products is critical for their biological activities and, as such, enzymes have evolved that specifically generate active stereoisomers. Lanthipeptides are post-translationally modified peptidic natural products that contain macrocyclic thioethers featuring lanthionine (Lan) and/or methyllanthionine (MeLan) residues with defined stereochemistry. In this report, we compare two class I lanthipeptide biosynthetic gene clusters (BGCs), <i>coi</i> and <i>olv</i>, that represent two families of lanthipeptide gene clusters found in Actinobacteria. The precursor peptides and BGCs are quite similar with genes encoding a dehydratase, cyclase, and methyltransferase (MT). We illustrate that the precursor peptide CoiA1 is converted by these enzymes into a poly"],"journal":["ACS chemical biology"],"pubmed_title":["Divergent Evolution of Lanthipeptide Stereochemistry."],"pmcid":["PMC9486935"],"funding_grant_id":["S10 RR027109 A","S10 RR027109","R37 GM058822"],"pubmed_authors":["van der Donk WA","Sarksian R"],"additional_accession":[]},"is_claimable":false,"name":"Divergent Evolution of Lanthipeptide Stereochemistry.","description":"The three-dimensional structure of natural products is critical for their biological activities and, as such, enzymes have evolved that specifically generate active stereoisomers. Lanthipeptides are post-translationally modified peptidic natural products that contain macrocyclic thioethers featuring lanthionine (Lan) and/or methyllanthionine (MeLan) residues with defined stereochemistry. In this report, we compare two class I lanthipeptide biosynthetic gene clusters (BGCs), <i>coi</i> and <i>olv</i>, that represent two families of lanthipeptide gene clusters found in Actinobacteria. The precursor peptides and BGCs are quite similar with genes encoding a dehydratase, cyclase, and methyltransferase (MT). We illustrate that the precursor peptide CoiA1 is converted by these enzymes into a poly","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2025-04-05T10:25:32.246Z","creation":"2025-04-05T10:25:32.246Z"},"accession":"S-EPMC9486935","cross_references":{"pubmed":["36001880"],"doi":["10.1021/acschembio.2c00492"]}}