Published in

American Society for Microbiology, Applied and Environmental Microbiology, 8(62), p. 2966-2969, 1996

DOI: 10.1128/aem.62.8.2966-2969.1996

Links

Tools

Export citation

Search in Google Scholar

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

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Green circle
Preprint: archiving allowed
Green circle
Postprint: archiving allowed
Orange circle
Published version: archiving restricted
Data provided by SHERPA/RoMEO

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A mutant of the peptide antibiotic nisin in which the dehydroalanine residue at position 5 has been replaced by an alanine has been produced and structurally characterized.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.