Literature DB >> 17240519

Thermodynamic properties of enzyme-catalyzed reactions involving cytosine, uracil, thymine, and their nucleosides and nucleotides.

Robert A Alberty1.   

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 Delta(f)G=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.

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Year:  2007        PMID: 17240519      PMCID: PMC1987330          DOI: 10.1016/j.bpc.2006.12.010

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  3 in total

1.  Biochemical thermodynamics: applications of Mathematica.

Authors:  Robert A Alberty
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2.  Thermodynamic properties of nucleotide reductase reactions.

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Journal:  Biochemistry       Date:  2004-08-03       Impact factor: 3.162

3.  Thermodynamic properties of enzyme-catalyzed reactions involving guanine, xanthine, and their nucleosides and nucleotides.

Authors:  Robert A Alberty
Journal:  Biophys Chem       Date:  2006-02-07       Impact factor: 2.352

  3 in total
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Journal:  J Phys Chem B       Date:  2010-05-06       Impact factor: 2.991

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  4 in total

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