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N‐terminal acetylation in paenibacillin, a novel lantibiotic
Author(s) -
He Zengguo,
Yuan Chunhua,
Zhang Liwen,
Yousef Ahmed E.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.07.008
Subject(s) - lantibiotics , paenibacillus polymyxa , acetylation , antibacterial peptide , chemistry , biochemistry , bacteria , antimicrobial peptides , peptide , bacteriocin , antimicrobial , microbiology and biotechnology , biology , genetics , antibacterial activity , gene
N‐terminal acetylation was uncovered in paenibacillin, a novel lantibiotic recently reported as a product of Paenibacillus polymyxa OSY‐DF. This N‐terminal modification is unprecedented among bacteria‐derived antimicrobial peptides and further illustrates the broad range of modifications that can occur in lantibiotics. Additionally, the primary structure of paenibacillin has been finally determined unequivocally by the extensive NMR analysis taken together with previous MS/MS results. These analyses revealed the structure of paenibacillin as one of the most post‐translationally modified lantibiotics.