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J Am Chem Soc. 2014 Sep 24;136(38):13150-3. doi: 10.1021/ja5070813. Epub 2014 Sep 10.

Structure and biosynthesis of carnolysin, a homologue of enterococcal cytolysin with D-amino acids.

Author information

1
Department of Chemistry, University of Alberta , Edmonton, Alberta, Canada , T6G 2G2.

Abstract

Lantibiotics are a group of highly post-translationally modified bacterial antimicrobial peptides characterized by the presence of the thioether-containing amino acids lanthionine and methyllanthionine. Carnobacterium maltaromaticum C2 was found to produce a two-component lantibiotic homologous to enterococcal cytolysin. Through tandem mass spectrometry and NMR spectroscopy, the post-translational modifications of carnolysin were established, and the topologies of the lanthionine and methyllanthionine rings were determined. Chiral GC-MS analysis revealed that, like cytolysin, carnolysin contained lanthionine and methyllanthionine residues of unusual stereochemistry. Carnolysin, unlike cytolysin, was shown to contain d-alanine and unprecedented D-aminobutyrate derived from serine and threonine, respectively. Carnolysin was heterologously expressed in Escherichia coli, demonstrating that reductase CrnJ is involved in the formation of the D-amino acids.

PMID:
25207953
DOI:
10.1021/ja5070813
[Indexed for MEDLINE]

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