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> | *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> | ||
*The <math>K_{eq}</math> value for the reactions that converts pyruvate has been defined as <math>3.32e^5</math> in <ref name="Owusu_2004">Owusu-Apenten R. ''Introduction to Food Chemistry'', First Edition, CRC Press (2004), ISBN-10: 084931724X </ref><center>[[File:Pyruvate_Keq.png|550px|link=]]</center> | *The <math>K_{eq}</math> value for the reactions that converts pyruvate has been defined as <math>3.32e^5</math> in <ref name="Owusu_2004">Owusu-Apenten R. ''Introduction to Food Chemistry'', First Edition, CRC Press (2004), ISBN-10: 084931724X </ref><center>[[File:Pyruvate_Keq.png|550px|link=]]</center> | ||
− | *The | + | *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>. | ||
− | *The <math>K_1</math> value calculated from the above mentioned values are | + | *The <math>K_1</math> value calculated from the above mentioned values are <math>2.20E-018</math> |
==Parameter values== | ==Parameter values== | ||
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! Remarks | ! Remarks | ||
|- | |- | ||
− | |<math> | + | |<math>K_1</math> |
− | |<math> | + | |<math><math>2.20E-018</math></math> |
− | | | + | | |
− | | | + | | |
|} | |} | ||
==References== | ==References== | ||
<references/> | <references/> |
Revision as of 12:07, 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 value for the reactions that converts pyruvate has been defined as Failed to parse (Cannot store math image on filesystem.): 3.32e^5
in [3]
- The Flux of pyruvate consumed by mitochondria measured for AS_30D is [4].
- 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.): <math>2.20E-018 </math> |
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
- ↑ Owusu-Apenten R. Introduction to Food Chemistry, First Edition, CRC Press (2004), ISBN-10: 084931724X
- ↑ Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 (doi)