ChemMedChem

Cover image for Vol. 12 Issue 14

Editorial Board Chairs: Karl-Heinz Altmann, Antonello Mai, Rainer Metternich. Editor: David Peralta

Impact Factor: 3.225

ISI Journal Citation Reports © Ranking: 2016: 17/60 (Chemistry Medicinal); 73/256 (Pharmacology & Pharmacy)

Online ISSN: 1860-7187

Associated Title(s): Angewandte Chemie International Edition, Chemistry - A European Journal, Chemistry – An Asian Journal, ChemBioChem, Medicinal Research Reviews, Molecular Informatics

June 15, 2010

VIP: Inhibition Studies of Mycobacterium tuberculosis Salicylate Synthase (MbtI)

VIP: Inhibition Studies of Mycobacterium tuberculosis Salicylate Synthase (MbtI)Alexandra Manos-Turvey, Esther M. M. Bulloch, Peter J. Rutledge, Edward N. Baker, J. Shaun Lott, and Richard J. Payne*

The first committed step in the biosynthesis of mycobactin T, a siderophore that is essential for the survival and virulence of M. tuberculosis, is catalyzed by salicylate synthase (MbtI). Therefore, the inhibition of MbtI would be an effective and highly specific mode of action for new anti-tuberculosis drugs. Payne and co-workers describe the first MbtI inhibition studies, using compounds that mimic the substrate and intermediates of the MbtI-catalyzed reaction. They found that mimics of isochorismate, the reaction intermediate, were the most potent MbtI inhibitors, effective in the low micromolar range. Their results indicate an important new direction in the development of compounds that combat tuberculosis infections.

Received March 30, 2010; published online June 10, 2010, DOI: 10.1002/cmdc.201000137.

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