[Ala4]surfactin, a novel isoform from Bacillus subtilis studied by mass and NMR spectroscopies.
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.
Peypoux
F
F
Laboratoire de Biochimie Microbienne, Université Claude Bernard Lyon 1, France.
Bonmatin
J M
JM
Labbe
H
H
Grangemard
I
I
Das
B C
BC
Ptak
M
M
Wallach
J
J
Michel
G
G
D000409:Alanine / Q000737:chemistry; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D002849:Chromatography, Gas; D002855:Chromatography, Thin Layer; D003470:Culture Media; D006868:Hydrolysis; D055666:Lipopeptides; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013500:Surface Tension; D013501:Surface-Active Agents / Q000737:chemistry; D014633:Valine / Q000737:chemistry
D001426:Bacterial Proteins; D003470:Culture Media; D055666:Lipopeptides; D010456:Peptides, Cyclic; D013501:Surface-Active Agents; C009365:surfactin peptide; D014633:Valine; D000409:Alanine