1996
DOI: 10.1007/bf00399421
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Protein engineering of lantibiotics

Abstract: Whereas protein engineering of enzymes and structural proteins nowadays is an established research tool for studying structure-function relationships of polypeptides and for improving their properties, the engineering of posttranslationally modified peptides, such as the lantibiotics, is just coming of age. The engineering of lantibiotics is less straightforward than that of unmodified proteins, since expression systems should be developed not only for the structural genes but also for the genes encoding the b… Show more

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Cited by 125 publications
(128 citation statements)
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“…The biological activity of lantibiotic peptides depends upon the formation of the correct ring structures (24)(25)(26)(27)(28) and the removal of the N-terminal leader sequence of the modified peptides (5,6). To investigate the biological activity of the haloduracin peptides prepared in vitro, the leader sequence of each product must therefore be removed.…”
Section: Resultsmentioning
confidence: 99%
“…The biological activity of lantibiotic peptides depends upon the formation of the correct ring structures (24)(25)(26)(27)(28) and the removal of the N-terminal leader sequence of the modified peptides (5,6). To investigate the biological activity of the haloduracin peptides prepared in vitro, the leader sequence of each product must therefore be removed.…”
Section: Resultsmentioning
confidence: 99%
“…Because the biosynthetic gene cluster for nisin (17,18) comprises only 11 genes, and that for the type B lantibiotic mersacidin (13,19) contains only 10, it is unlikely that all 21 of the genes described here are involved in the production of cinnamycin.…”
Section: Resultsmentioning
confidence: 99%
“…The observation that the presence of a 2-hydroxyalanine residue at position 5 reduces the growth-inhibiting effect of nisin seems to be in contrast with the observation of Liu and Hansen (1992) that [AlaS]subtilin, a bacteriocin closely related to nisin, exhibits an unimpaired growth-inhibiting activity but a strongly reduced spore-killing effect. In the case of nisin, [AlaSInisin and [Ala5, Ala33lnisin were reported to have an unimpaired growth-inhibiting activity (Dodd and Gasson, 1994;Kuipers et al, 1996). The three-dimensional structure of nisin in water and in membrane-mimicking micelles shows a clearly amphipathic character for the Nterminal part of the molecule (van de Ven et al, 1991 ;van den Hooven et al, 1996a).…”
Section: Discussionmentioning
confidence: 99%
“…This indicates that Dha5 or an intact ring A is essential for the functional properties of nisin. It has been reported that [AlaSInisin and [ A M , Ala331nisin have normal biological activities (Dodd and Gasson, 1994 ;Kuipers et al, 1996). [Ala5]subtilin, a bacteriocin structurally very similar to nisin, was reported to have an unimpaired growth-inhibiting activity but a strongly reduced spore-killing effect (Liu and Hansen, 1992).…”
mentioning
confidence: 99%