Peypoux F, Bonmatin J M, Labbe H, Grangemard I, Das B C, Ptak M, Wallach J, Michel G
Laboratoire de Biochimie Microbienne, Université Claude Bernard Lyon 1, France.
Eur J Biochem. 1994 Aug 15;224(1):89-96. doi: 10.1111/j.1432-1033.1994.tb19998.x.
When Bacillus subtilis S 499 was grown on a culture medium containing L-alanine as nitrogen source, a mixture of surfactins was obtained. Suitable chromatographic conditions allowed the separation of isoforms. Among these compounds, a new variant of surfactin was isolated and its structure was established by chemical and spectrometric methods, especially by NMR spectrometry. It contains a peptide sequence which differs from that of standard surfactin by the replacement of the L-valine residue by L-alanine residue in position 4. The folding mode of [Ala4]surfactin as deduced from NMR results was compared with that of standard surfactin and the structure/properties relationship issuing from the study of this new isoform is discussed.
