| Literature DB >> 20580404 |
Randy B Stockbridge1, Gottfried K Schroeder, Richard Wolfenden.
Abstract
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. 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID： 20580404 PMCID： PMC2918718 DOI： 10.1016/j.bioorg.2010.05.003
Source DB: PubMed Journal: Bioorg Chem ISSN： 0045-2068 Impact factor: 5.275