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

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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Geissler S,Götz F,Kupke T

doi

10.1128/jb.178.1.284-288.1996

subject

Has Abstract

pub_date

1996-01-01 00:00:00

pages

284-8

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

178

pub_type

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