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Chem Biol. 2011 Jul 29;18(7):857-67. doi: 10.1016/j.chembiol.2011.05.007.

Biosynthesis of the antimicrobial peptide epilancin 15X and its N-terminal lactate.

Author information

1
Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.

Abstract

Lantibiotics are ribosomally synthesized and posttranslationally 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.

PMID:
21802007
PMCID:
PMC3161514
DOI:
10.1016/j.chembiol.2011.05.007
[Indexed for MEDLINE]
Free PMC Article

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