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Analysis of the products of a PKS mutant specifically inactivated in the dehydratase domain of extension\u2010module 1 showed that this module catalyzes two successive elongations with different outcomes. Strikingly, the enoylreductase domain of this module can apparently be \u201ctoggled\u201d off and on : it functions in only the second of these two cycles. This novel mechanism expands our understanding of PKS assembly\u2010line catalysis and may explain examples of apparent non\u2010colinearity in other modular PKS systems.<\/jats:p>","DOI":"10.1002\/anie.201701220","type":"journal-article","created":{"date-parts":[[2017,4,18]],"date-time":"2017-04-18T09:28:49Z","timestamp":1492507729000},"page":"5503-5506","source":"Crossref","is-referenced-by-count":32,"title":["An Iterative Module in the Azalomycin\u2005F Polyketide Synthase Contains a Switchable Enoylreductase Domain"],"prefix":"10.1002","volume":"56","author":[{"given":"Wei","family":"Xu","sequence":"first","affiliation":[{"name":"Key Laboratory of Combinatorial Biosynthesis and Drug Discovery (Wuhan University) Ministry of Education, and School of Pharmaceutical Sciences Wuhan University  185 East Lake Road Wuhan 430071 P.R. 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