Difference between revisions of "Adenylate kinase"
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Adenylate kinase is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides. | Adenylate kinase is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides. | ||
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|2.26 <ref name="Hernandez2011"></ref> | |2.26 <ref name="Hernandez2011"></ref> | ||
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| + | ==Parameters with uncertainty== | ||
| + | {|class="wikitable" | ||
| + | ! Parameter | ||
| + | ! Value | ||
| + | |- | ||
| + | | <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>: | ||
| + | <math>Keq(ATP+AMP \rightarrow 2*ADP, pH=7.4, T=25^oC)=2.26</math><br/> | ||
| + | In Mass action rate law the relationship is <math>\frac{K_2}{K_1} = K_{eq}</math>. Considering <math>K_{eq} = 2.26</math> we have <math>K_2=2.26</math> and <math>K_1 = 1</math> to be consistent with the equation. The value of <math>K_1</math> and <math>K_2</math> would be varied based on the uncertainty on <math>K_{eq}</math> value mentioned in the following table. The percentage of error in Keq is <math>\approx 4</math>. With similar percent of error the value for <math>K_1 = 1 \pm 0.04</math> and <math>K_2 = 2.26 \pm 0.09044</math> | ||
| + | |} | ||
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| + | === Equilibrium constant === | ||
| + | {|class="wikitable" | ||
| + | ! 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 [[http://xpdb.nist.gov/enzyme_thermodynamics/enzyme_data1.pl?T1=61ATK/BUR_640 61ATK/BUR_640]] from Atkinson et al. (1961) <ref name="atkinson61">Atkinson, M. R., Burton, R. M. and Morton, R. K. (1961) Biochem J. 78(4):813–820. ([http://www.ncbi.nlm.nih.gov/pubmed/13684980 pmid: 13684980])</ref> Table 2<br/> | ||
| + | Therefore, Keq(forward) = 0.48 +/-0.015 (n=7; mean+/-SEM calculated from individual measurements). | ||
| + | |} | ||
| + | |||
| + | ==References== | ||
| + | <references/> | ||
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
![K_{1}[ATP][AMP] - K_{2}[ADP]^2](/wiki/images/math/7/f/c/7fc054b0299ef7cf1db75a18a2860588.png)
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]:
|
. Considering 
we have 
and 
to be consistent with the equation. The value of 
value mentioned in the following table. The percentage of error in Keq is 
. With similar percent of error the value for 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)
