Copurification and characterization of deacetoxycephalosporin C synthetase/hydroxylase from Cephalosporium acremonium.

@article{Dotzlaf1987CopurificationAC,
  title={Copurification and characterization of deacetoxycephalosporin C synthetase/hydroxylase from Cephalosporium acremonium.},
  author={Joe E. Dotzlaf and W K Yeh},
  journal={Journal of bacteriology},
  year={1987},
  volume={169 4},
  pages={1611-8}
}
Deacetoxycephalosporin C synthetase (expandase), which catalyzes ring expansion of penicillin N to deacetoxycephalosporin C (DAOC), has been stabilized in vitro and purified to near homogeneity from the industrially important fungus Cephalosporium acremonium. Throughout the purification, the expandase activity remained physically associated with and in a constant ratio of 7:1 to DAOC hydroxylase activity. The latter activity mediates hydroxylation of DAOC to deacetylcephalosporin C (DAC). The… CONTINUE READING

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References

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Showing 1-6 of 6 references

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

  • M. M. Bradford
  • Anal. Biochem. 72:248-254
  • 1976

a-Ketoadipate-coupled dioxygenases, p. 167-214

  • M. T. Abbott, S. Udenfriend
  • 1974

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