Difference between revisions of "Mitocondrial pyruvate metabolism"
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*The rate law is defined as <center><math>v = K_1[Pyruvate][ADP]^{13}[Pi]^{13}\left(1-\frac{\frac{[ATP]^{13}}{[Pyruvate][ADP]^{13}[Pi]^{13}}}{K_{eq}}\right)</math></center><br> | *The rate law is defined as <center><math>v = K_1[Pyruvate][ADP]^{13}[Pi]^{13}\left(1-\frac{\frac{[ATP]^{13}}{[Pyruvate][ADP]^{13}[Pi]^{13}}}{K_{eq}}\right)</math></center><br> | ||
− | *The <math>\Delta G^o{'}</math> for the reaction that converts Pyruvate to Acetyl-CoA is <math>\Delta G^ | + | *The <math>\Delta G^o{'}</math> for the reaction that converts Pyruvate to Acetyl-CoA is <math>\Delta G^o{'}= -33.4 Kj/Mol</math>. Therefore, the overall standard free-energy change for Pyruvate metabolism is <math>\Delta G^o{'}= -63.9 Kj/Mol</math>. Calculating <math>K_{eq}</math> value from these free energy gives <math>\Delta G' = - 20.9\ kJ.mol^{-1}</math>, <math>Keq = exp(-\frac{\Delta G'}{RT}) = exp(\frac{20900}{8.31*298.15}) \approx 4908</math> |
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*The Flux of pyruvate consumed by mitochondria measured for AS_30D is <math> v = 1.8</math> <ref name="Hernandez2011"> Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 ([http://dx.doi.org/10.1016/j.bbabio.2010.11.006 doi])</ref>. | *The Flux of pyruvate consumed by mitochondria measured for AS_30D is <math> v = 1.8</math> <ref name="Hernandez2011"> Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 ([http://dx.doi.org/10.1016/j.bbabio.2010.11.006 doi])</ref>. | ||
*The steady state concentrations for substrates and products are <math>ATP=8.7 \pm 3 (5)</math>, <math>ADP = 2.7 \pm 1.3</math>, <math>Pyruvate = 8.5 \pm 3.6</math> and <math>Pi = 7.5</math>. | *The steady state concentrations for substrates and products are <math>ATP=8.7 \pm 3 (5)</math>, <math>ADP = 2.7 \pm 1.3</math>, <math>Pyruvate = 8.5 \pm 3.6</math> and <math>Pi = 7.5</math>. |
Revision as of 12:47, 12 May 2014
Mitocondrial pyruvate metabolism(MPM) is an enzyme that generates ATP form pyruvate.
Chemical reaction
Rate equation
- Chemical reactions proceed to equilibrium within closed systems. For a simple reaction it is defined as where forward and reverse rates are equal.
- Equilibrium is not reached in open system due to influx and outflux. Mass action ratio[1] for reaction is defined as where subscript ob represents observable at a given point.
- Deviation from equilibrium is measured with Disequilibrium constant as
- Given the simple uni molecular reaction the mass action equation can be modified as
Considering and we have,
- The generalized arbitrary mass action ratio gives us
For eg. for the reaction , the rate law would be
- This equation demonstrates how a rate expression can be divided into parts that include both kinetics and thermodynamic properties [2].
- Given the net rate of reaction , we have
In this model
- The rate law is defined as
- The Failed to parse (Cannot store math image on filesystem.): \Delta G^o{'} for the reaction that converts Pyruvate to Acetyl-CoA is Failed to parse (Cannot store math image on filesystem.): \Delta G^o{'}= -33.4 Kj/Mol . Therefore, the overall standard free-energy change for Pyruvate metabolism is Failed to parse (Cannot store math image on filesystem.): \Delta G^o{'}= -63.9 Kj/Mol . Calculating value from these free energy gives ,
- The Flux of pyruvate consumed by mitochondria measured for AS_30D is [3].
- The steady state concentrations for substrates and products are , , and .
- The value calculated from the above mentioned values are Failed to parse (Cannot store math image on filesystem.): 2.20E-018
Parameter values
Parameter | Value | Organism | Remarks |
---|---|---|---|
Failed to parse (Cannot store math image on filesystem.): 2.20E^{-018} |
References
- ↑ Hess B. and Brand K. (1965), Enzymes and metabolite profiles. In Control of energy metabolism. III. Ed. B. Chance, R. K. Estabrook and J. R. Williamson. New York: Academic Press
- ↑ Sauro H M, Enzyme Kinetics for Systems Biology, Second Edition, Ambrosius Publishing (2013), ISBN-10: 0-9824773-3-3
- ↑ Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 (doi)