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

被引:55
作者
Chan, WC
Dodd, HM
Horn, N
Maclean, K
Lian, LY
Bycroft, BW
Gasson, MJ
Roberts, GCK
机构
[1] UNIV LEICESTER, BIOL NMR CTR, LEICESTER LE1 9HN, LEICS, ENGLAND
[2] UNIV NOTTINGHAM, DEPT PHARMACEUT SCI, NOTTINGHAM NG7 2RD, ENGLAND
[3] FOOD RES INST, NORWICH, NORFOLK, ENGLAND
[4] UNIV LEICESTER, DEPT BIOCHEM, LEICESTER LE1 9HN, LEICS, ENGLAND
关键词
D O I
10.1128/AEM.62.8.2966-2969.1996
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A mutant of the peptide antibiotic nisin in which the dehydroalanine residue at position 5 has been replaced by an alanine has been produced and structurally characterized, It is shown to have activity very similar to that of wild-type nisin in inhibiting growth of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.
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收藏
页码:2966 / 2969
页数:4
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