{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang SA"],"funding":["HHS | NIH | National Institute of General Medical Sciences","Welch Foundation","NIH HHS","NIGMS NIH HHS"],"pagination":["24794-24801"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7547251"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["117(40)"],"pubmed_abstract":["The structure of lincomycin A consists of the unusual eight-carbon thiosugar core methyllincosamide (MTL) decorated with a pendent <i>N</i>-methylprolinyl moiety. Previous studies on MTL biosynthesis have suggested GDP-ᴅ-<i>erythro</i>-α-ᴅ-<i>gluco</i>-octose and GDP-ᴅ-α-ᴅ-lincosamide as key intermediates in the pathway. However, the enzyme-catalyzed reactions resulting in the conversion of GDP-ᴅ-<i>erythro</i>-α-ᴅ-<i>gluco</i>-octose to GDP-ᴅ-α-ᴅ-lincosamide have not yet been elucidated. Herein, a biosynthetic subpathway involving the activities of four enzymes-LmbM, LmbL, CcbZ, and CcbS (the LmbZ and LmbS equivalents in the closely related celesticetin pathway)-is reported. These enzymes catalyze the previously unknown biosynthetic steps including 6-epimerization, 6,8-dehydration, 4-epim"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Studies of lincosamide formation complete the biosynthetic pathway for lincomycin A."],"pmcid":["PMC7547251"],"funding_grant_id":["GM035906","R37 GM035906","S10 OD021508","R01 GM035906","F-1511"],"pubmed_authors":["Zhang J","Wang SA","Liu HW","Sasaki E","Ushimaru R","Lin CI"],"additional_accession":[]},"is_claimable":false,"name":"Studies of lincosamide formation complete the biosynthetic pathway for lincomycin A.","description":"The structure of lincomycin A consists of the unusual eight-carbon thiosugar core methyllincosamide (MTL) decorated with a pendent <i>N</i>-methylprolinyl moiety. Previous studies on MTL biosynthesis have suggested GDP-ᴅ-<i>erythro</i>-α-ᴅ-<i>gluco</i>-octose and GDP-ᴅ-α-ᴅ-lincosamide as key intermediates in the pathway. However, the enzyme-catalyzed reactions resulting in the conversion of GDP-ᴅ-<i>erythro</i>-α-ᴅ-<i>gluco</i>-octose to GDP-ᴅ-α-ᴅ-lincosamide have not yet been elucidated. Herein, a biosynthetic subpathway involving the activities of four enzymes-LmbM, LmbL, CcbZ, and CcbS (the LmbZ and LmbS equivalents in the closely related celesticetin pathway)-is reported. These enzymes catalyze the previously unknown biosynthetic steps including 6-epimerization, 6,8-dehydration, 4-epim","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2025-04-18T13:42:04.582Z","creation":"2025-04-06T23:28:07.066Z"},"accession":"S-EPMC7547251","cross_references":{"pubmed":["32958639"],"doi":["10.1073/pnas.2009306117"]}}