Todd L. Lowary and colleagues at the University of Alberta, Canada, have synthesised a series of UDP-galactofuranose analogs and used these analogs to examine enzyme–substrate binding interactions for the galactofuranosyltransferase enzyme GlfT2, a glycosyltransferase responsible for the formation of the galactan complex in M. tuberculosis and a potential drug target.
Critical hydrogen bonding interactions within the active site of the mycobacterial galactofuranosyltransferase GlfT2 are revealed and it is hoped the knowledge of these specific protein-carbohydrate interactions may be explored for the development of novel inhibitors.
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Synthetic UDP-galactofuranose analogs reveal critical enzyme–substrate interactions in GlfT2-catalyzed mycobacterial galactan assembly
Myles B. Poulin, Ruokun Zhou and Todd L. Lowary
Org. Biomol. Chem., 2012, Advance Article
DOI: 10.1039/C2OB25159K, Paper
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Todd L. Lowary’s OBC work is also highlighted in this C&EN news story ‘Determining Sugar Sequence Fidelity’ |
