• M M Yakimov
    Department of Microbiology, GBF National Research Center for Biotechnology, Mascheroder Weg 1, 38124, Braunschweig, Germany.
  • W R Abraham
  • Holger Meyer
    GBF-Gesellschaft fuer Biotechnologische Forschung
  • Laura Giuliano
  • P N Golyshin

The structural characterization of the cyclic lipoheptapeptide surfactant lichenysin A components, produced by Bacillus licheniformis strains via the non-ribosomal pathway on a corresponding peptide synthetase, was carried out using a tandem mass spectrometry (MS/MS) under fast atom bombardment (FAB) conditions. Based on the analysis of the collision-induced fragment-ion spectrum of the single charged molecular ions of both native and partially hydrolyzed forms of lipopeptide, a new general structure of lichenysin A components was elucidated. It varies from previously proposed structure by having in the peptide portion of lipopeptide the L-Gln-1 and L-Asp-5 residues instead of L-Glu-1 and L-Asn-5. The verified chemical structure of lichenysin A was found to be reflected in the structural organization of the corresponding lichenysin A synthetase, LchA, described recently.

Keywords

  • Bacillus/chemistry, Lipoproteins/chemistry, Molecular Structure, Peptides, Cyclic/chemistry, Spectrometry, Mass, Fast Atom Bombardment
Original languageEnglish
Pages (from-to)273-80
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)
Volume1438
Issue number2
Publication statusPublished - 18 May 1999
View graph of relations