The rate of spontaneous cleavage of the glycosidic bond of adenosine.
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 3.7x10(-12)s(-1) at 25 degrees C, and the rate enhancement generated by the corresponding glycoside hydrolase is approximately 5x10(12)-fold.
Stockbridge
Randy B
RB
Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, 27599, United States.
Schroeder
Gottfried K
GK
Wolfenden
Richard
R
D000241:Adenosine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics
D000241:Adenosine