期刊
FEBS LETTERS
卷 582, 期 18, 页码 2787-2792出版社
WILEY
DOI: 10.1016/j.febslet.2008.07.008
关键词
lantibiotics; paenibacillin; NMR; N-terminal acetylation; antibacterial peptides
资金
- NCRR NIH HHS [RR08299] Funding Source: Medline
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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