Difference between revisions of "Pyruvate kinase"
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The rate equation is represented by the allosteric regualation model of [http://en.wikipedia.org/wiki/MWC_model Monod, Wyman and Changeux] (MWS). [http://en.wikipedia.org/wiki/Fructose_1,6-bisphosphatase Fru1,6BP] and [http://en.wikipedia.org/wiki/Serine Serine] are activators and [http://en.wikipedia.org/wiki/Adenosine_triphosphate ATP] is inhibiting. Simple [http://en.wikipedia.org/wiki/Michaelis%E2%80%93Menten_kinetics Micahelis-Menten kinetics] (Briggs Haldane) is used for ADP and reverse reaction <ref name="MWC_1965"> Monod J, Wyman J, Changeux J-P (1965) On the Nature of Allosteric Transitions: A Plausible Model . Journal of Molecular Biology 12:88–118 ([http://dx.doi.org/10.1016/S0022-2836(65)80285-6 doi]) </ref> | The rate equation is represented by the allosteric regualation model of [http://en.wikipedia.org/wiki/MWC_model Monod, Wyman and Changeux] (MWS). [http://en.wikipedia.org/wiki/Fructose_1,6-bisphosphatase Fru1,6BP] and [http://en.wikipedia.org/wiki/Serine Serine] are activators and [http://en.wikipedia.org/wiki/Adenosine_triphosphate ATP] is inhibiting. Simple [http://en.wikipedia.org/wiki/Michaelis%E2%80%93Menten_kinetics Micahelis-Menten kinetics] (Briggs Haldane) is used for ADP and reverse reaction <ref name="MWC_1965"> Monod J, Wyman J, Changeux J-P (1965) On the Nature of Allosteric Transitions: A Plausible Model . Journal of Molecular Biology 12:88–118 ([http://dx.doi.org/10.1016/S0022-2836(65)80285-6 doi]) </ref> | ||
− | <center><math>V_m \left( \left(\frac{\frac{[ADP]}{K_{ADP}}}{1+\frac{[ADP]}{K_{ADP}}}\right) \left( \frac{\frac{[PEP]}{ | + | <center><math>V_m \left( \left(\frac{\frac{[ADP]}{K_{ADP}}}{1+\frac{[ADP]}{K_{ADP}}}\right) \left( \frac{\frac{[PEP]}{Km_{PEP}}\left( 1+\frac{[PEP]}{Km_{PEP}} \right)^3 }{ \frac{L \left( 1 + \frac{[ATP]}{Ki_{ATP}} \right)^4 }{ \left( 1 + \frac{[SER]}{Ka_{SER}} \right)^4 \left( 1 + \frac{F1,6BP}{Ka_{F1,6BP}} \right)^4 } + \left( 1 + \frac{[PEP]}{Km_{PEP}} \right)^4} \right) - \left( \frac{\frac{[ATP][PYR]}{K_{ATP} \times K_{PYR} \times K_{eq}}}{\frac{[ATP]}{K_{ATP}} + \frac{[PYR]}{K_{PYR}} + \frac{[ATP][PYR]}{K_{ATP} \times K_{PYR} } + 1} \right) \right)</math></center> |
==Parameter values== | ==Parameter values== |
Revision as of 17:05, 4 March 2014
Pyruvate kinase is a transferase enzyme that catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP.
Contents
Chemical reaction
![PEP + ADP \rightleftharpoons Pyrvate + ATP](/wiki/images/math/6/a/e/6aefc45d5babff149006084e4e37f222.png)
Rate equation
The rate equation is represented by the allosteric regualation model of Monod, Wyman and Changeux (MWS). Fru1,6BP and Serine are activators and ATP is inhibiting. Simple Micahelis-Menten kinetics (Briggs Haldane) is used for ADP and reverse reaction [1]
![V_m \left( \left(\frac{\frac{[ADP]}{K_{ADP}}}{1+\frac{[ADP]}{K_{ADP}}}\right) \left( \frac{\frac{[PEP]}{Km_{PEP}}\left( 1+\frac{[PEP]}{Km_{PEP}} \right)^3 }{ \frac{L \left( 1 + \frac{[ATP]}{Ki_{ATP}} \right)^4 }{ \left( 1 + \frac{[SER]}{Ka_{SER}} \right)^4 \left( 1 + \frac{F1,6BP}{Ka_{F1,6BP}} \right)^4 } + \left( 1 + \frac{[PEP]}{Km_{PEP}} \right)^4} \right) - \left( \frac{\frac{[ATP][PYR]}{K_{ATP} \times K_{PYR} \times K_{eq}}}{\frac{[ATP]}{K_{ATP}} + \frac{[PYR]}{K_{PYR}} + \frac{[ATP][PYR]}{K_{ATP} \times K_{PYR} } + 1} \right) \right)](/wiki/images/math/2/3/1/231eb04d3df21c7d241c848f5fb72e82.png)
Parameter values
Parameter | Value | Organism | Remarks |
---|---|---|---|
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3 | HeLa cell line | |
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195172 | ||
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0.014 | ||
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0.4 | ||
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10 | ||
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0.86 | ||
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2.5 | ||
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1 | ||
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