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J Am Chem Soc. 2008 May 28;130(21):6706-7. doi: 10.1021/ja8018687. Epub 2008 May 1.

Inhibitors of UDP-galactopyranose mutase thwart mycobacterial growth.

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Departments of Chemistry and Biochemistry, University of WisconsinMadison, Madison, Wisconsin 53706, USA.


Galactofuranose (Galf) residues are fundamental components of the cell wall of mycobacteria. A key enzyme, UDP-galactopyranose mutase (UGM), that participates in Galf incorporation mediates isomerization of UDP-Galf from UDP-galactopyranose (UDP-Galp). UGM is of special interest as a therapeutic target because the gene encoding it is essential for mycobacterial viability and there is no comparable enzyme in humans. We used structure-activity relationships and molecular design to devise UGM inhibitors. From a focused library of synthetic aminothiazoles, several compounds that block the UGM from Klebsiella pneumoniae or Mycobacterium tuberculosis were identified. These inhibitors block the growth of M. smegmatis.

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