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Structure of Ddn, the Deazaflavin-Dependent Nitroreductase from Mycobacterium tuberculosis Involved in Bioreductive Activation of PA-824

Year: 2013

Type: article

Abstract: (Structure 20, 101–112, January 11, 2012) The original article unfortunately has an author error in the units for kcat and kcat/Km on page 108. In Table 2, row 2, all kcat and kcat/Km units should be “min−1” and “min−1μM−1,” respectively, rather than be “s−1” and “s−1μM−1.” The scientific interpretations remain the same, only the units change. Our conclusions about the active site structure based on the kinetic analysis of the mutants do not change. Structure of Ddn, the Deazaflavin-Dependent Nitroreductase from Mycobacterium tuberculosis Involved in Bioreductive Activation of PA-824Cellitti et al.StructureJanuary 11, 2012In BriefTuberculosis continues to be a global health threat, making bicyclic nitroimidazoles an important new class of therapeutics. A deazaflavin-dependent nitroreductase (Ddn) from Mycobacterium tuberculosis catalyzes the reduction of nitroimidazoles such as PA-824, resulting in intracellular release of lethal reactive nitrogen species. The N-terminal 30 residues of Ddn are functionally important but are flexible or access multiple conformations, preventing structural characterization of the full-length, enzymatically active enzyme. Full-Text PDF Open Access

Source: Structure

DOI: 10.1016/j.str.2012.12.012