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. 2003 Jan;47(1):378-82.
doi: 10.1128/AAC.47.1.378-382.2003.

Drug targeting Mycobacterium tuberculosis cell wall synthesis: development of a microtiter plate-based screen for UDP-galactopyranose mutase and identification of an inhibitor from a uridine-based library

Michael S Scherman  1 , Katharine A Winans, Richard J Stern, Victoria Jones, Carolyn R Bertozzi, Michael R McNeil
Affiliations

Drug targeting Mycobacterium tuberculosis cell wall synthesis: development of a microtiter plate-based screen for UDP-galactopyranose mutase and identification of an inhibitor from a uridine-based library

Michael S Scherman et al. Antimicrob Agents Chemother. 2003 Jan.

Abstract

A microtiter plate assay for UDP-galactopyranose mutase, an essential cell wall biosynthetic enzyme of Mycobacterium tuberculosis, was developed. The assay is based on the release of tritiated formaldehyde from UDP-galactofuranose but not UDP-galactopyranose by periodate and was used to identify a uridine-based enzyme inhibitor from a chemical library.

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Figures

FIG. 1.
FIG. 1.
(A) Conversion of UDP-galactopyranose to UDP-galactofuranose as catalyzed by UDP-galactopyranose mutase (Glf, Rv3809c). (B) Structure of M. tuberculosis arabinogalactan demonstrating the key structural role of galactofuranosyl residues.
FIG. 2.
FIG. 2.
Assay for UDP-galactopyranose mutase. UDP-galf, but not UDP-galp, forms neutral tritiated formaldehyde when treated with sodium periodate.
FIG. 3.
FIG. 3.
Activity of 320KAW73 (A) and its precursors (B and C). The data shown are averages of values.
FIG. 4.
FIG. 4.
Comparison of 320KAW73 with related compounds in the screening library that were inactive.
See this image and copyright information in PMC

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