Journal
CHEMISTRY & BIOLOGY
Volume 18, Issue 7, Pages 857-867Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2011.05.007
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Funding
- National Institutes of Health [GM58822]
- National Institutes of Health under Ruth L. Kirschstein National Research Service [T32 GM070421]
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Lantibiotics are ribosomally synthesized and post-translationally modified antimicrobial peptides. The recently discovered lantibiotic epilancin 15X produced by Staphylococcus epidermidis 15X154 contains an unusual N-terminal lactate group. To understand its biosynthesis, the epilancin 15X biosynthetic gene cluster was identified. The N-terminal lactate is produced by dehydration of a serine residue in the first position of the core peptide by ElxB, followed by proteolytic removal of the leader peptide by ElxP and hydrolysis of the resulting new N-terminal dehydroalanine. The pyruvate group thus formed is reduced to lactate by an NADPH-dependent oxidoreductase designated ElxO. The enzymatic activity of ElxB, ElxP, and ElxO were investigated in vitro or in vivo and the importance of the N-terminal modification for peptide stability against bacterial aminopeptidases was assessed.
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