Journal
FEBS LETTERS
Volume 582, Issue 18, Pages 2787-2792Publisher
WILEY
DOI: 10.1016/j.febslet.2008.07.008
Keywords
lantibiotics; paenibacillin; NMR; N-terminal acetylation; antibacterial peptides
Funding
- NCRR NIH HHS [RR08299] Funding Source: Medline
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N-terminal acetylation was uncovered in paenibacillin, a novel lantibiotic recently reported as a product of Paenibacillus polymyxa OSY-DF. This N-terminal modi. cation is unprecedented among bacteria-derived antimicrobial peptides and further illustrates the broad range of modi. cations 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. Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.
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