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Issue 8, 2014
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Sulfonium ions as inhibitors of the mycobacterial galactofuranosyltransferase GlfT2

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Abstract

The mycobacterial cell wall possesses a core galactan moiety composed of approximately 30 galactofuranosyl residues attached via alternating β-(1→5) and β-(1→6) linkages. A bifunctional galactofuranosyltransferase, GlfT2, is one of two essential enzymes for mycobacterial cell wall biosynthesis. The enzymatic reactions catalyzed by GlfT2 undoubtedly proceed by way of a transition state that has significant oxocarbenium-ion character. In this paper, a series of sulfonium ion compounds were designed and synthesized as analogues of the donor substrate, uridine diphosphate-galactofuranose, as potential inhibitors of GlfT2. The compounds contain moieties that mimic both galactofuranose and uridine diphosphate domains, and carry a permanent positive charge to mimic the oxocarbenium ion-like transition state. These compounds were evaluated against Glf2 using a coupled spectrophotometric assay, and some were shown to be weak inhibitors of the enzyme.

Graphical abstract: Sulfonium ions as inhibitors of the mycobacterial galactofuranosyltransferase GlfT2

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Supplementary files

Article information


Submitted
19 Feb 2014
Accepted
11 Mar 2014
First published
12 Mar 2014

This article is Open Access

Med. Chem. Commun., 2014,5, 1130-1137
Article type
Concise Article

Sulfonium ions as inhibitors of the mycobacterial galactofuranosyltransferase GlfT2

J. Li and T. L. Lowary, Med. Chem. Commun., 2014, 5, 1130
DOI: 10.1039/C4MD00067F

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