BIOL 82 |
| The Nudix hydrolases cleave nucleoside diphosphates linked to some moiety, x, and are identified by the common signature sequence: GX5E7REUXEEXGU (U= I, L, or V). Rv2985 diadenosine polyphosphatase from M. tuberculosis is a homolog to diadenosine polyphosphatase “invasion enzymes” from other pathogenic bacteria. Rv2985 cleaves Ap4A, Ap5A and Ap6A with nearly comparable activity. Characteristic of Nudix hydrolases, Rv2985 requires a divalent metal cofactor and has an alkaline pH optimum. Regardless of the substrate, ATP is always a resulting product, and it is always the fourth phosphorus from one of the adenosines which is attacked during hydrolysis. We have subcloned and purified a His-tagged protein, which retains full expression, solubility, and activity, as compared to wild type, and purifies by affinity chromatography as one pure band. Blocking the ability of a pathogen such as M. tuberculosis to be able to invade its human host may be an excellent target for the development of new antibiotics. Supported by an NIH AREA grant. |
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Frontiers in Chemical Biology
5:00 PM-7:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biological Chemistry |