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Solution Structure of the Quaternary MutT−M 2+ −AMPCPP−M 2+ Complex and Mechanism of Its Pyrophosphohydrolase Action †,‡

✍ Scribed by Lin, Jian; Abeygunawardana, Chitrananda; Frick, David N.; Bessman, Maurice J.; Mildvan, Albert S.


Book ID
126042790
Publisher
American Chemical Society
Year
1997
Tongue
English
Weight
430 KB
Volume
36
Category
Article
ISSN
0006-2960

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Solution structure, mutagenesis, and NH
✍ 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