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Issue 30, 2014
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Bis-chlorination of a hexapeptide–PCP conjugate by the halogenase involved in vancomycin biosynthesis

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Abstract

Vancomycin is an important nosocomial antibiotic containing a glycosylated, cross-linked and doubly chlorinated heptapeptide backbone. During the biosynthesis of the vancomycin aglycone, two β-hydroxytyrosine (Bht) residues are inserted at positions-2 and -6 into the heptapeptide backbone by a non-ribosomal peptide synthetase. A single flavin-dependent chlorinase (VhaA) is responsible for chlorinating both Bht residues at some ill-defined point in the assembly process. We show here using in vitro assays that VhaA is able to introduce a chlorine atom into each aromatic ring of both Bht residues at positions-2 and -6 of a peptide carrier protein-bound hexapeptide. The results suggest that VhaA can recognize and chlorinate two quite different sites within a linear hexapeptide intermediate during vancomycin biosynthesis.

Graphical abstract: Bis-chlorination of a hexapeptide–PCP conjugate by the halogenase involved in vancomycin biosynthesis

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Supplementary files

Article information


Submitted
03 Mar 2014
Accepted
15 Apr 2014
First published
23 Apr 2014

This article is Open Access

Org. Biomol. Chem., 2014,12, 5574-5577
Article type
Communication
Author version available

Bis-chlorination of a hexapeptide–PCP conjugate by the halogenase involved in vancomycin biosynthesis

P. C. Schmartz, K. Zerbe, K. Abou-Hadeed and J. A. Robinson, Org. Biomol. Chem., 2014, 12, 5574
DOI: 10.1039/C4OB00474D

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