来自表皮葡萄球菌的丝氨酸蛋白酶EpiP催化表皮菌素前体肽的加工过程。
Serine protease EpiP from Staphylococcus epidermidis catalyzes the processing of the epidermin precursor peptide.
作者信息
Geissler S, Götz F, Kupke T
机构信息
Universität Tübingen, Federal Republic of Germany.
出版信息
J Bacteriol. 1996 Jan;178(1):284-8. doi: 10.1128/jb.178.1.284-288.1996.
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.
摘要
研究了丝氨酸蛋白酶EpiP在表皮菌素生物合成中的作用。表皮菌素作为一种52个氨基酸的前体肽EpiA合成，该前体肽经过翻译后修饰并加工成成熟的22个氨基酸的肽抗生素。epiP通过木糖调节表达载体pCX15在肉葡萄球菌中表达。通过反相色谱法和随后的电喷雾质谱法跟踪含有EpiP的肉葡萄球菌（pCX15epiP）培养滤液对未修饰的EpiA前体肽切割成前导肽和前表皮菌素的过程。
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