Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage.

@article{Corts1995RepositioningOA,
  title={Repositioning of a domain in a modular polyketide synthase to promote specific chain cleavage.},
  author={Jes{\'u}s Ayala Cort{\'e}s and K E Wiesmann and Gwen Roberts and Martin C. Brown and James C Staunton and Peter Francis Leadlay},
  journal={Science},
  year={1995},
  volume={268 5216},
  pages={1487-9}
}
Macrocyclic polyketides exhibit an impressive range of medically useful activities, and there is great interest in manipulating the genes that govern their synthesis. The 6-deoxyerythronolide B synthase (DEBS) of Saccharopolyspora erythraea, which synthesizes the aglycone core of the antibiotic erythromycin A, has been modified by repositioning of a chain-terminating cyclase domain to the carboxyl-terminus of DEBS1, the multienzyme that catalyzes the first two rounds of polyketide chain… CONTINUE READING

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