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. 1996 Jan;178(1):284–288. doi: 10.1128/jb.178.1.284-288.1996

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

S Geissler 1, F Götz 1, T Kupke 1
PMCID: PMC177651  PMID: 8550430

Abstract

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 followed by reversed-phase chromatography and subsequent electrospray mass spectrometry.

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Selected References

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