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

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:A mutant of the peptide antibiotic nisin in which the dehydroalanine residue at position 5 has been replaced by an alanine has been produced and structurally characterized.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

journal_name

Appl Environ Microbiol

authors

Chan WC,Dodd HM,Horn N,Maclean K,Lian LY,Bycroft BW,Gasson MJ,Roberts GC

doi

10.1128/AEM.62.8.2966-2969.1996

subject

Has Abstract

pub_date

1996-08-01 00:00:00

pages

2966-9

issue

8

eissn

0099-2240

issn

1098-5336

journal_volume

62

pub_type

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