期刊
CHEMISTRY & BIOLOGY
卷 18, 期 4, 页码 438-444出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2011.02.007
关键词
-
资金
- BMBF [FKZ0313805J/FKZ0315585A/FKZ03155811]
- DFG [SFB 642]
In the biosynthesis of complex polyketides, acyltransferase domains (ATs) are key determinants of structural diversity. Their specificity and position in polyketide synthases (PKSs) usually controls the location and structure of building blocks in polyketides. Many bioactive polyketides, however, are generated by trans-AT PKSs lacking internal AT domains. They were previously believed to use mainly malonyl-specific free-standing ATs. Here, we report a mechanism of structural diversification, in which the trans-AT KirCII regiospecifically incorporates the unusual extender unit ethylmalonyl-CoA in kirromycin polyketide biosynthesis.
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