Serine protease EpiP from Staphylococcus epidermidis catalyzes the processing of the epidermin precursor peptide.

@article{Geissler1996SerinePE,
  title={Serine protease EpiP from Staphylococcus epidermidis catalyzes the processing of the epidermin precursor peptide.},
  author={Steffen Geissler and Friedrich G{\"o}tz and Thomas Kupke},
  journal={Journal of bacteriology},
  year={1996},
  volume={178 1},
  pages={284-8}
}
The function of serine protease EpiP in epidermin biosynthesis was investigated. Epidermin is synthesized as a 52-amino-acid precursor peptide, EpiA, which is posttranslationally modified and processed to the mature 22-amino-acid peptide antibiotic. epiP was expressed in Staphylococcus carnosus with xylose-regulated expression vector pCX15. The cleavage of the unmodified EpiA precursor peptide to leader peptide and proepidermin by EpiP-containing culture filtrates of S. carnosus (pCX15epiP) was… CONTINUE READING