Structure and catalytic mechanism of the thioesterase CalE7 in enediyne biosynthesis.

@article{Kotaka2009StructureAC,
  title={Structure and catalytic mechanism of the thioesterase CalE7 in enediyne biosynthesis.},
  author={Masayo Kotaka and Rong Kong and Insaf Qureshi and Qin Shi Ho and Huihua Sun and Chong Wai Liew and Lan Pei Goh and Peter W Cheung and Yuguang Mu and Julien Lescar and Zhao-Xun Liang},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 23},
  pages={15739-49}
}
The biosynthesis of the enediyne moiety of the antitumor natural product calicheamicin involves an iterative polyketide synthase (CalE8) and other ancillary enzymes. In the proposed mechanism for the early stage of 10-membered enediyne biosynthesis, CalE8 produces a carbonyl-conjugated polyene with the assistance of a putative thioesterase (CalE7). We have determined the x-ray crystal structure of CalE7 and found that the subunit adopts a hotdog fold with an elongated and kinked substrate… CONTINUE READING
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