Difference between revisions of "Adenylate kinase"
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==Parameters with uncertainty== | ==Parameters with uncertainty== | ||
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+ | ! Parameter | ||
+ | ! Value | ||
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| k<sub>1</sub>=442, k<sub>2</sub>=1000 | | k<sub>1</sub>=442, k<sub>2</sub>=1000 | ||
| The kinetic parameters of adenylate kinase are unknown. Therefore, it was modeled using mass action kinetics with parameters k1 and k2 consistent with the equilibrium constant of the reaction. The equilibrium constant (Keq=0.442) 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 kinetic parameters of adenylate kinase are unknown. Therefore, it was modeled using mass action kinetics with parameters k1 and k2 consistent with the equilibrium constant of the reaction. The equilibrium constant (Keq=0.442) 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>: | ||
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== Equilibrium constant == | == Equilibrium constant == | ||
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! Equilibrium constant | ! Equilibrium constant | ||
! Conditions | ! Conditions |
Revision as of 11:06, 6 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 |
---|---|
k1=442, k2=1000 | The kinetic parameters of adenylate kinase are unknown. Therefore, it was modeled using mass action kinetics with parameters k1 and k2 consistent with the equilibrium constant of the reaction. The equilibrium constant (Keq=0.442) 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)