Literature DB >> 15792796

Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis.

Miquel B Ekkelenkamp1, Micha Hanssen, Shang-Te Danny Hsu, Ad de Jong, Dana Milatovic, Jan Verhoef, Nico A J van Nuland.   

Abstract

The potential application of lantibiotics as food-preserving agents and more recently as antibiotics has strongly increased the interest in these antibacterial peptides. Here, we report the elucidation of the primary and three-dimensional structures of the novel lantibiotic epilancin 15X from Staphylococcus epidermidis using high-resolution nuclear magnetic resonance spectroscopy and tandem mass spectrometry. The molecule contains ten post-translationally modified amino acids, three lanthionine ring structures and a hydroxy-propionyl N-terminal moiety. The primary and tertiary structure and the distribution of positive charges are closely similar to the previously identified lantibiotic epilancin K7, most likely indicative of a common mode of action.

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Year:  2005        PMID: 15792796     DOI: 10.1016/j.febslet.2005.01.083

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  25 in total

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6.  Biosynthesis of the antimicrobial peptide epilancin 15X and its N-terminal lactate.

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