| Literature DB >> 8550430 |
S Geissler1, F Götz, T Kupke.
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.Entities:
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Year: 1996 PMID: 8550430 PMCID: PMC177651 DOI: 10.1128/jb.178.1.284-288.1996
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490