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

被引:54
作者
Geissler, S [1 ]
Gotz, F [1 ]
Kupke, T [1 ]
机构
[1] UNIV TUBINGEN,D-72076 TUBINGEN,GERMANY
关键词
D O I
10.1128/jb.178.1.284-288.1996
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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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收藏
页码:284 / 288
页数:5
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