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U.S.A."],"published-print":{"date-parts":[[2015,8,18]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    Sulfur incorporation into natural products remains poorly understood except for those derived from intact cysteine or methionine. Leinamycin (LNM) is a sulfur-containing antitumor antibiotic featuring an unusual 1,3-dioxo-1,2-dithiolane moiety. A pyridoxal phosphate-dependent domain, termed cysteine lyase (SH) domain, is identified within the LNM polyketide synthase (PKS) module-8 of LnmJ. The LnmJ-SH domain catalyzes C-S bond cleavage by using\n                    <jats:sc>l<\/jats:sc>\n                    -cysteine and\n                    <jats:sc>l<\/jats:sc>\n                    -cysteine\n                    <jats:italic>S<\/jats:italic>\n                    -modified analogs as substrates, shares no sequence homology with any other enzymes catalyzing C-S bond cleavage, and represents a new family of PKS domains. This study establishes\n                    <jats:sc>l<\/jats:sc>\n                    -cysteine as the origin of the C-3 sulfur of LNM, expands the chemistry and enzymology of PKS, and sets the stage to incorporate sulfur into polyketide natural products by PKS engineering.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1508437112","type":"journal-article","created":{"date-parts":[[2015,8,3]],"date-time":"2015-08-03T22:49:47Z","timestamp":1438642187000},"page":"10359-10364","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":45,"title":["C-S bond cleavage by a polyketide synthase domain"],"prefix":"10.1073","volume":"112","author":[{"given":"Ming","family":"Ma","sequence":"first","affiliation":[{"name":"Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeremy R.","family":"Lohman","sequence":"additional","affiliation":[{"name":"Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tao","family":"Liu","sequence":"additional","affiliation":[{"name":"Division of Pharmaceutical Sciences, University of Wisconsin-Madison, Madison, WI 53705;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ben","family":"Shen","sequence":"additional","affiliation":[{"name":"Department of Chemistry, The Scripps Research Institute, Jupiter, FL 33458;"},{"name":"Division of Pharmaceutical Sciences, University of Wisconsin-Madison, Madison, WI 53705;"},{"name":"Department of Molecular Therapeutics, The Scripps Research Institute, Jupiter, FL 33458;"},{"name":"Natural Products Library Initiative at The Scripps Research Institute, The Scripps Research Institute, Jupiter, FL 33458"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2015,8,3]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nchembio779","article-title":"Trafficking in persulfides: Delivering sulfur in biosynthetic pathways","volume":"2","author":"Mueller EG","year":"2006","unstructured":"EG Mueller, Trafficking in persulfides: Delivering sulfur in biosynthetic pathways. 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