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However, the enzymology of their formation has not been completely established. Now it is demonstrated that TxnO9, a CalC\u2010like protein belonging to a START family, functions as an unexpected anthraquinone\u2010\u03b3\u2010pyrone synthase involved in the biosynthesis of antitumor antibiotic trioxacarcin\u2005A (TXN\u2010A). Structural analysis by NMR identified a likely substrate\/product\u2010binding mode and putative key active sites of TxnO9, which allowed an enzymatic mechanism to be proposed. Moreover, a subset of uncharacterized homologous proteins bearing an unexamined Lys\u2010Thr dyad exhibit the same function. Therefore, the functional assignment and mechanistic investigation of this \u03b3\u2010pyrone synthase elucidated an undescribed step in TXN\u2010A biosynthesis, and the discovery of this new branch of polyketide heterocyclases expands the functions of the START superfamily.<\/jats:p>","DOI":"10.1002\/anie.201806729","type":"journal-article","created":{"date-parts":[[2018,8,29]],"date-time":"2018-08-29T13:20:29Z","timestamp":1535548829000},"page":"13475-13479","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Enzymology of Anthraquinone\u2010\u03b3\u2010Pyrone Ring Formation in Complex Aromatic Polyketide Biosynthesis"],"prefix":"10.1002","volume":"57","author":[{"given":"Xian\u2010Feng","family":"Hou","sequence":"first","affiliation":[{"name":"State Key Laboratory of Bioorganic and Natural Products Chemistry, Center for Excellence in Molecular Synthesis Shanghai Institute of Organic Chemistry Chinese Academy of 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