J. Bacteriol., 01 1996, 284-288, Vol 178, No. 1
Copyright © 1996, American Society for Microbiology

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

S Geissler, F Gotz and T Kupke
Universitat Tubingen, Federal Republic of Germany.

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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