Difference between revisions of "Adenylate kinase"
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− | | <math>K_1=1</math>, <math>K_2=2.26</math> | + | | <math>K_1=1 \pm 0.04</math>, <math>K_2=2.26 \pm 0.09044</math> |
| The Adenylate kinase was modeled using mass action kinetics with parameters <math>K_1</math> and <math>K_2</math> consistent with the equilibrium constant of the reaction. The equilibrium constant (Keq=2.26) is from Bergmeyer H.U. (1974) page 486<ref name="bergmeyer74">Bergmeyer H.U. (1974) ''Methods of enzymatic analysis'', Publisher: Verlag Chemie (vol 1)</ref>: | | The Adenylate kinase was modeled using mass action kinetics with parameters <math>K_1</math> and <math>K_2</math> consistent with the equilibrium constant of the reaction. The equilibrium constant (Keq=2.26) is from Bergmeyer H.U. (1974) page 486<ref name="bergmeyer74">Bergmeyer H.U. (1974) ''Methods of enzymatic analysis'', Publisher: Verlag Chemie (vol 1)</ref>: | ||
<math>Keq(ATP+AMP \rightarrow 2*ADP, pH=7.4, T=25^oC)=2.26</math><br/> | <math>Keq(ATP+AMP \rightarrow 2*ADP, pH=7.4, T=25^oC)=2.26</math><br/> |
Latest revision as of 16:38, 28 May 2014
Adenylate kinase is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides.
Contents
Chemical equation
Rate equation
Reversible mass action rate law is used
Parameter values
Parameter | Value | Organism | Remarks |
---|---|---|---|
1 [1] | HeLa cell line | ||
2.26 [1] |
Parameters with uncertainty
Parameter | Value |
---|---|
, | The Adenylate kinase was modeled using mass action kinetics with parameters and consistent with the equilibrium constant of the reaction. The equilibrium constant (Keq=2.26) is from Bergmeyer H.U. (1974) page 486[2]:
|
Equilibrium constant
Equilibrium constant | Conditions | Source |
---|---|---|
0.48+/-0.015 (mean+/-SEM; n=7) | pH=7, T=25°C, 10mM Mg2+ | NIST database "Thermodynamics of Enzyme-Catalyzed Reactions" entry [61ATK/BUR_640] from Atkinson et al. (1961) [3] Table 2 Therefore, Keq(forward) = 0.48 +/-0.015 (n=7; mean+/-SEM calculated from individual measurements). |
References
- ↑ 1.0 1.1 Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 (doi)
- ↑ Bergmeyer H.U. (1974) Methods of enzymatic analysis, Publisher: Verlag Chemie (vol 1)
- ↑ Atkinson, M. R., Burton, R. M. and Morton, R. K. (1961) Biochem J. 78(4):813–820. (pmid: 13684980)