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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1969 Mar;62(3):952–956. doi: 10.1073/pnas.62.3.952

DEHYDROALANYLLYSINE: IDENTICAL COOH-TERMINAL STRUCTURES IN THE PEPTIDE ANTIBIOTICS NISIN AND SUBTILIN

Erhard Gross 1,2, John L Morell 1,2, Lyman C Craig 1,2
PMCID: PMC223691  PMID: 5257015

Abstract

The recent finding of α,β-unsaturated amino acid residues by Gross and Morrel in the polypeptide antibiotic nisin has stimulated a wider investigation of other antibiotic peptides, particularly those known to contain lanthionine. Subtilin is similar to nisin in that it polymerizes easily and contains lanthionine and β-methyl lanthionine. Like nisin it was found to contain a carboxyl terminal dehydroalanyllysine sequence and to be split by the enzyme nisinase. An additional α,β-unsaturated amino acid residue was shown to be present in subtilin by reaction with excess methyl mercaptoacetate and subsequent hydrolysis and amino acid analysis. Nisin contains three dehydropeptide residues.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BODANSZKY M., PERLMAN D. ARE PEPTIDE ANTIBIOTICS SMALL PROTEINS? Nature. 1964 Nov 28;204:840–844. doi: 10.1038/204840a0. [DOI] [PubMed] [Google Scholar]
  2. Craig L. C., Stewart K. Dialysis. X. On thin film countercurrent dialysis. Biochemistry. 1965 Dec;4(12):2712–2719. doi: 10.1021/bi00888a022. [DOI] [PubMed] [Google Scholar]
  3. Gross E., Morell J. L. The number and nature of alpha,beta-unsaturated amino acids in nisin. FEBS Lett. 1968 Nov;2(1):61–64. doi: 10.1016/0014-5793(68)80101-2. [DOI] [PubMed] [Google Scholar]
  4. Gross E., Morell J. L. The presence of dehydroalanine in the antibiotic nisin and its relationship to activity. J Am Chem Soc. 1967 May 24;89(11):2791–2792. doi: 10.1021/ja00987a084. [DOI] [PubMed] [Google Scholar]
  5. Jarvis B. Resistance to nisin and production of nisin-inactivating enzymes by several Bacillus species. J Gen Microbiol. 1967 Apr;47(1):33–48. doi: 10.1099/00221287-47-1-33. [DOI] [PubMed] [Google Scholar]
  6. Sheehan J. C., Mania D., Nakamura S., Stock J. A., Maeda K. The structure of telomycin. J Am Chem Soc. 1968 Jan 17;90(2):462–470. doi: 10.1021/ja01004a043. [DOI] [PubMed] [Google Scholar]

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