Mutational, NMR, and NH Exchange Studies of the Tight and Selective Binding of 8-Oxo-dGMP by the MutT Pyrophosphohydrolase †

Solution structure, mutagenesis, and NH

Solution structure, mutagenesis, and NH exchange studies of the MutT enzyme–Mg2+-8-oxo-dGMP complex

✍ M.A. Massiah; V. Saraswat; H.F. Azurmendi; A.S. Mildvan 📂 Article 📅 2004 🏛 Elsevier Science 🌐 English ⚖ 335 KB

The MutT pyrophosphohydrolase from E. coli (129 residues) catalyzes the hydrolysis of nucleoside triphosphates (NTP), including 8-oxo-dGTP, by substitution at Pb, to yield NMP and pyrophosphate. The product, 8-oxo-dGMP is an unusually tight binding, slowly exchanging inhibitor with a K D ¼ 52 nM, (D