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Retro\u2010biosynthetic analysis suggests that the backbone of galbonolides is assembled by a type I modular polyketide synthase (PKS). Unexpectedly, the galbonolide biosynthetic gene cluster, <jats:italic>gbn<\/jats:italic>, in <jats:italic>Streptomyces<\/jats:italic> sp. LZ35 encodes a hybrid fatty acid synthase (FAS)\u2010PKS pathway. In vitro reconstitution revealed the functions of GbnA (an AT\u2010ACP didomain protein), GbnC (a FabH\u2010like enzyme), and GbnB (a novel multidomain PKS module without AT and ACP domains) responsible for assembling the backbone of galbonolides, respectively. To our knowledge, this study is the first biochemical characterization of a hybrid FAS\u2010PKS pathway for the biosynthesis of 14\u2010membered macrolides. The identification of this pathway provides insights into the evolution of PKSs and could facilitate the design of modular pools for synthetic biology.<\/jats:p>","DOI":"10.1002\/cbic.201500017","type":"journal-article","created":{"date-parts":[[2015,3,3]],"date-time":"2015-03-03T15:33:10Z","timestamp":1425396790000},"page":"998-1007","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["In Vitro Reconstitution of a PKS Pathway for the Biosynthesis of Galbonolides in <i>Streptomyces<\/i> sp. 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