Structure-activity relationships in the peptide antibiotic nisin: Role of dehydroalanine 5

W. C. Chan, H. M. Dodd, N. Horn, K. Maclean, L. Y. Lian, B. W. Bycroft, M. J. Gasson, G. C K Roberts

    Research output: Contribution to journalArticlepeer-review

    Abstract

    A mutant of the peptide antibiotic nisin in which the dehydroalanine residue at position 5 has been replaced by an alanine has been produced and structurally characterized. It is shown to have activity very similar to that of wild-type nisin in inhibiting growth of Lactococcus lactis and Micrococcus luteus but is very much less active than nisin as an inhibitor of the outgrowth of spores of Bacillus subtilis. These observations, which parallel those of W. Liu and J. N. Hansen (Appl. Environ. Microbiol. 59:648-651, 1993) on the corresponding mutant of the related antibiotic subtilin, are discussed in terms of the mechanism(s) of action of these antibiotics.
    Original languageEnglish
    Pages (from-to)2966-2969
    Number of pages3
    JournalApplied and environmental microbiology
    Volume62
    Issue number8
    Publication statusPublished - Aug 1996

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