Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis.

@article{Korman2010StructureAF,
  title={Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis.},
  author={Tyler Paz Korman and Jason M Crawford and Jason W. Labonte and Adam G. Newman and Justin F. Wong and Craig A Townsend and Shiou-Chuan Tsai},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 14},
  pages={6246-51}
}
Polyketide natural products possess diverse architectures and biological functions and share a subset of biosynthetic steps with fatty acid synthesis. The final transformation catalyzed by both polyketide synthases (PKSs) and fatty acid synthases is most often carried out by a thioesterase (TE). The synthetic versatility of TE domains in fungal nonreducing, iterative PKSs (NR-PKSs) has been shown to extend to Claisen cyclase (CLC) chemistry by catalyzing C-C ring closure reactions as opposed to… CONTINUE READING

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