| Range |
-10.9 kcal/mol
|
| Organism |
Generic |
| Reference |
Dickson KS, Burns CM, Richardson JP. Determination of the free-energy change for repair of a DNA phosphodiester bond. J Biol Chem. 2000 May 26 275(21):15828-31. P.15831 left column 3rd paragraph and right column top paragraphPubMed ID10748184
|
| Primary Source |
[8] Frey PA, Arabshahi A. Standard free energy change for the hydrolysis of the alpha, beta-phosphoanhydride bridge in ATP. Biochemistry. 1995 Sep 12 34(36):11307-10.PubMed ID7547856
|
| Method |
Primary source p.11307 left column bottom paragraph: "Upon consulting the literature, [investigators] have found that the standard free energy change for the hydrolysis of ATP to AMP and PPi is much more negative than the conventional value and much more negative than that for the hydrolysis of ATP to ADP and Pi." |
| Comments |
P.15831 left column 3rd paragraph: "The standard free energy of ATP hydrolysis to form AMP and PPi, recently re-evaluated by Frey and Arabshahi (primary source), is −10.9 kcal/mol in 1 mM Mg2+. Using the formulas of Alberty (ref 9), this value is −11.6 kcal/mol in 10 mM Mg2+, the concentration of Mg2+ present in these studies." P.15831 right column top paragraph: "The value used for the standard free energy of hydrolysis of ATP to form AMP and PPi was recently re-evaluated by Frey and Arabshahi (primary source). The value reported of -10.9 kcal/mol is significantly higher than the values of -7.7 to -8.4 kcal/mol listed in many biochemistry textbooks." |
| Entered by |
Uri M |
| ID |
111336 |