103960-10-7Relevant articles and documents
The rate of spontaneous cleavage of the glycosidic bond of adenosine
Stockbridge, Randy B.,Schroeder, Gottfried K.,Wolfenden, Richard
experimental part, p. 224 - 228 (2010/10/01)
Previous estimates of the rate of spontaneous cleavage of the glycosidic bond of adenosine were determined by extrapolating the rates of the acid- and base-catalyzed reactions to neutral pH. Here we show that cleavage also proceeds through a pH-independent mechanism. Rate constants were determined as a function of temperature at pH 7 and a linear Arrhenius plot was constructed. Uncatalyzed cleavage occurs with a rate constant of 3.7 × 10-12 s-1 at 25 °C, and the rate enhancement generated by the corresponding glycoside hydrolase is ~5 × 1012-fold.