Title of article :
Thermodynamic properties of enzyme-catalyzed reactions involving cytosine, uracil, thymine, and their nucleosides and nucleotides Original Research Article
Author/Authors :
Robert A. Alberty، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Abstract :
The standard Gibbs energies of formation of species in the cytidine triphosphate series, uridine triphosphate series, and thymidine triphosphate series have been calculated on the basis of the convention that ΔfG = 0 for the neutral form of cytidine in aqueous solution at 298.15 K at zero ionic strength. This makes it possible to calculate apparent equilibrium constants for a number of reactions for which apparent equilibrium constants have not been measured or cannot be measured because they are too large. This paper adds fifteen reactants to the database BasicBiochemData3 at MathSource that includes 199 reactants. The standard transformed Gibbs energies of formation of these fifteen reactants are used to calculate apparent equilibrium constants at 298.15 K, ionic strength 0.25 M, and pHs 5, 6, 7, 8, and 9 for thirty two reactions. The pKs, standard Gibbs energies of hydrolysis, and standard Gibbs energies of deamination are given for these fifteen reactants.
Keywords :
Cytosine , Thymine , Apparent equilibrium constants , Uracil , thermodynamics , Nucleotides
Journal title :
Biophysical Chemistry
Journal title :
Biophysical Chemistry