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Posttranslationally modified bacteriocins—the lantibiotics
Author(s) -
Guder André,
Wiedemann Imke,
Sahl HansGeorg
Publication year - 2000
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2000)55:1<62::aid-bip60>3.0.co;2-y
Subject(s) - lantibiotics , lanthionine , bacteriocin , nisin , chemistry , biochemistry , lipid ii , biosynthesis , dehydroalanine , amino acid , enzyme , organic chemistry , antimicrobial
Lantibiotics are a subgroup of bacteriocins that are characterized by the presence of the unusual thioether amino acids lanthionine and 3‐methyllanthionine generated through posttranslational modification. The biosynthesis of lantibiotics follows a defined pathway comprising modifications of the prepeptide, proteolytic activation, and export. The genes encoding the biosynthesis apparatus and the lantibiotic prepeptide are organized in clusters, which also include information for proteins involved in regulation and producer self‐protection. The elongated cationic lantibiotics primarily act through the formation of pores and recent progress with nisin and epidermin has shown that specific docking molecules such as lipid II play an essential role in this mechanism. Mersacidin and actagardine inhibit cell wall biosynthesis by complexing the precursor lipid II, whereas the cinnamycin‐like peptides bind to phosphoethanolamine thus inhibiting phospholipase A2. © 2000 John Wiley & Sons, Inc. Biopoly 55: 62–73, 2000