Difference between revisions of "Pyruvate kinase"
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==Parameters with uncertainty== | ==Parameters with uncertainty== | ||
+ | |||
+ | |||
+ | {|class="wikitable" | ||
+ | ! Parameter | ||
+ | ! Value | ||
+ | ! Units | ||
+ | ! Organism | ||
+ | ! Remarks | ||
+ | |- | ||
+ | |<math>V_{mf}</math> | ||
+ | |1.9<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> | ||
+ | |<math> \text{mM min}^{-1} </math> | ||
+ | |rowspan="10"|HeLa cell line | ||
+ | | | ||
+ | |- | ||
+ | |<math>K_{eq}</math><ref name="Hernandez2011"></ref> | ||
+ | |195172 | ||
+ | | | ||
+ | |Recalculated from the ΔGº´ = - 31.4 KJ mol-1. | ||
+ | |- | ||
+ | |<math>Km_{PEP}</math><ref name="Hernandez2011"></ref> | ||
+ | |0.014 | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>Km_{ADP}</math><ref name="Hernandez2011"></ref> | ||
+ | |0.4 | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>Km_{PYR}</math><ref name="Bergmeyer_1983">H.U. Bergmeyer. ''Methods of Enzymatic Analysis''. Verlag Chemie, Winheim</ref> | ||
+ | |10 | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>Km_{ATP}</math><ref name="Bergmeyer_1983"></ref> | ||
+ | |0.86 | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>Ka_{F1,6BP}</math><ref name="Imamura_1982">Imamura K, Tanaka T (1982). ''Pyruvate kinase isoenzymes from rat'', Methods Enzymol. 90 (1982) 150–165 </ref> | ||
+ | |<math>4\times 10^{-4}</math> | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>Ki_{ATP}</math><ref name="Imamura_1982"></ref> | ||
+ | |2.5 | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>L</math><ref name="arbitrary">Arbitrary value</ref> | ||
+ | |1 | ||
+ | |Dimensionless | ||
+ | |- | ||
+ | |<math>Ka_{SER}</math> | ||
+ | |5 | ||
+ | |mM | ||
+ | | For allosteric regulation the affinity constant is used. It is the inverted dissociation constant. so <math> Ka_{SER} = \frac{1}{K_d}</math> where <math> k_d = 0.2 mM</math> <ref name="Chaneton_2012>Chaneton, B. ''et al.''(2012) ''Serine is a natural ligand and allosteric activator of pyruvate kinase M2''. Nature 491, 458–462 </ref> | ||
+ | |} | ||
+ | |||
+ | |||
==References== | ==References== | ||
<references/> | <references/> |
Revision as of 14:24, 30 April 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=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}}}{1 +\frac{[ATP]}{K_{ATP}} + \frac{[PYR]}{K_{PYR}} + \frac{[ATP][PYR]}{K_{ATP} \times K_{PYR} }} \right) \right)](/wiki/images/math/6/0/8/608585715d214881c663ba97b3810b40.png)
Parameter values
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
![]() |
1.9[2] | ![]() |
HeLa cell line | |
![]() |
195172 | Recalculated from the ΔGº´ = - 31.4 KJ mol-1. | ||
![]() |
0.014 | mM | ||
![]() |
0.4 | mM | ||
![]() |
10 | mM | ||
![]() |
0.86 | mM | ||
![]() |
![]() |
mM | ||
![]() |
2.5 | mM | ||
![]() |
1 | Dimensionless | ||
![]() |
5 | mM | For allosteric regulation the affinity constant is used. It is the inverted dissociation constant. so ![]() ![]() |
Parameters with uncertainty
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
![]() |
1.9[2] | ![]() |
HeLa cell line | |
![]() |
195172 | Recalculated from the ΔGº´ = - 31.4 KJ mol-1. | ||
![]() |
0.014 | mM | ||
![]() |
0.4 | mM | ||
![]() |
10 | mM | ||
![]() |
0.86 | mM | ||
![]() |
![]() |
mM | ||
![]() |
2.5 | mM | ||
![]() |
1 | Dimensionless | ||
![]() |
5 | mM | For allosteric regulation the affinity constant is used. It is the inverted dissociation constant. so ![]() ![]() |
References
- ↑ Monod J, Wyman J, Changeux J-P (1965). On the Nature of Allosteric Transitions: A Plausible Model . Journal of Molecular Biology 12:88–118 (doi)
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 (doi)
- ↑ 3.0 3.1 3.2 3.3 H.U. Bergmeyer. Methods of Enzymatic Analysis. Verlag Chemie, Winheim
- ↑ 4.0 4.1 4.2 4.3 Imamura K, Tanaka T (1982). Pyruvate kinase isoenzymes from rat, Methods Enzymol. 90 (1982) 150–165
- ↑ 5.0 5.1 Arbitrary value
- ↑ 6.0 6.1 Chaneton, B. et al.(2012) Serine is a natural ligand and allosteric activator of pyruvate kinase M2. Nature 491, 458–462