학술논문
Structure and Biosynthesis of Carnolysin, a Homologue of Enterococcal Cytolysin with D-Amino Acids.
Document Type
Article
Source
Subject
*BIOSYNTHESIS
*AMINO acids
*AMINO compounds
*LANTHIONINE
*MASS spectrometry
*ALANINE
*ESCHERICHIA coli
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Language
ISSN
0002-7863
Abstract
Lantibiotics are a group of highly posttranslationally 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 twocomponent 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. [ABSTRACT FROM AUTHOR]