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Chemical Compound Review

Mycosubtilin     3-[ (3S,6S,13S,16R,19R,22R,25R,28S )-6,13,19...

Synonyms: Mycosubtiline, LS-93773, AC1MJ13T, 1392-60-5, 59112-50-4
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Production of Mycosubtilin


High impact information on Mycosubtilin

  • Comparison of the sequences flanking the mycosubtilin operon of B. subtilis ATCC6633, with the complete genome sequence of B. subtilis strain 168 indicates that the fengycin and mycosubtilin lipopeptide synthetase operons are exchanged between the two B. subtilis strains [1].
  • The gene cluster from B. subtilis ATCC6633 specifying the biosynthesis of mycosubtilin was identified [1].
  • Mycosubtilin overproduction by Bacillus subtilis BBG100 enhances the organism's antagonistic and biocontrol activities [3].
  • The biological activity of the iturin lipopeptides is modulated by the primary structure of the peptide cycle as illustrated by the methylation of the D-Tyr2 residue which dramatically decreases the activity or by the inversion of the two adjacent Ser6-Asn7 residues which makes mycosubtilin more active than iturin A [4].
  • The structure of mycosubtilin, a peptidolipid antibiotic from Bacillus subtilis, was revised by FAB mass spectrometry, 2D NMR spectrometry and also by Edman degradation of the peptide resulting from the N-bromosuccinimide reaction [5].
  • Mycosubtilin alone, at the air–water interface, forms a monolayer film and keeps its turn conformation. In the presence of DMPC, mycosubtilin binds to phospholipid monolayers, in a surface pressure-dependent manner [6].

Biological context of Mycosubtilin

  • Comparison of the amino acid sequences encoded by the iturin A operon and the mycosubtilin operon revealed that ituD, ituA, and ituB have high levels of homology to the counterpart genes fenF (79%), mycA (79%), and mycB (79%), respectively [7].

Anatomical context of Mycosubtilin


Associations of Mycosubtilin with other chemical compounds


  1. The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a multifunctional hybrid between a peptide synthetase, an amino transferase, and a fatty acid synthase. Duitman, E.H., Hamoen, L.W., Rembold, M., Venema, G., Seitz, H., Saenger, W., Bernhard, F., Reinhardt, R., Schmidt, M., Ullrich, C., Stein, T., Leenders, F., Vater, J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  2. Action of mycosubtilin and of bacillomycin L on Micrococcus luteus cells and protoplasts: influence of the polarity of the antibiotics upon their action on the bacterial cytoplasmic membrane. Besson, F., Peypoux, F., Michel, G. FEBS Lett. (1978) [Pubmed]
  3. Mycosubtilin overproduction by Bacillus subtilis BBG100 enhances the organism's antagonistic and biocontrol activities. Leclère, V., Béchet, M., Adam, A., Guez, J.S., Wathelet, B., Ongena, M., Thonart, P., Gancel, F., Chollet-Imbert, M., Jacques, P. Appl. Environ. Microbiol. (2005) [Pubmed]
  4. Iturins, a special class of pore-forming lipopeptides: biological and physicochemical properties. Maget-Dana, R., Peypoux, F. Toxicology (1994) [Pubmed]
  5. Revised structure of mycosubtilin, a peptidolipid antibiotic from Bacillus subtilis. Peypoux, F., Pommier, M.T., Marion, D., Ptak, M., Das, B.C., Michel, G. J. Antibiot. (1986) [Pubmed]
  6. Interactions of the natural antimicrobial mycosubtilin with phospholipid membrane models. Nasir, M.N., Thawani, A., Kouzayha, A., Besson, F. Colloids. Surf. B. Biointerfaces. (2010) [Pubmed]
  7. Cloning, sequencing, and characterization of the iturin A operon. Tsuge, K., Akiyama, T., Shoda, M. J. Bacteriol. (2001) [Pubmed]
  8. Iturin lipopeptides: interactions of mycosubtilin with lipids in planar membranes and mixed monolayers. Maget-Dana, R., Ptak, M. Biochim. Biophys. Acta (1990) [Pubmed]
  9. Action of mycosubtilin on erythrocytes and artificial membranes. Besson, F., Quentin, M.J., Michel, G. Microbios (1989) [Pubmed]
  10. Action of mycosubtilin, an antifungal antibiotic of Bacillus subtilis, on the cell membrane of Saccharomyces cerevisiae. Besson, F., Michel, G. Microbios (1989) [Pubmed]
  11. Molecular characterization and analysis of the operon encoding the antifungal lipopeptide bacillomycin D. Moyne, A.L., Cleveland, T.E., Tuzun, S. FEMS Microbiol. Lett. (2004) [Pubmed]
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