Difference between revisions of "Pyruvate kinase"
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− | |<math>L</math><ref name="del_valle">del Valle,P.,de Arriaga, D., Busto, F. and Soler, J. (1986) ''A study of the allosteric kinetics of Phycomyces pyruvate kinase as judged by the effect of e-alanine and fructose 1,6-bisphosphate''. Biochim. Biophys. Acta 874, 193-204</ref | + | |<math>L</math> |
− | + | |<math>3200 \pm 275</math><ref name="del_valle">del Valle,P.,de Arriaga, D., Busto, F. and Soler, J. (1986) ''A study of the allosteric kinetics of Phycomyces pyruvate kinase as judged by the effect of e-alanine and fructose 1,6-bisphosphate''. Biochim. Biophys. Acta 874, 193-204</ref> | |
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Revision as of 16:52, 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
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]
Parameter values
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
1.9[2] | HeLa cell line | |||
[2] | 195172 | Recalculated from the ΔGº´ = - 31.4 KJ mol-1. | ||
[2] | 0.014 | mM | ||
[2] | 0.4 | mM | ||
[3] | 10 | mM | ||
[3] | 0.86 | mM | ||
[4] | mM | |||
[4] | 2.5 | mM | ||
[5] | 1 | Dimensionless | ||
5 | mM | For allosteric regulation the affinity constant is used. It is the inverted dissociation constant. so where [6] |
Parameters with uncertainty
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
[7] | HeLa cell line | |||
[2] | 195172 | Recalculated from the ΔGº´ = - 31.4 KJ mol-1. | ||
Failed to parse (Cannot store math image on filesystem.): 0.17 \pm 0.01 [8] | mM | |||
[8] | mM | |||
[3] | 10 | mM | ||
[3] | 0.86 | mM | ||
[4] | mM | |||
[4] | 2.5 | mM | ||
[9] | Dimensionless | |||
5 | mM | For allosteric regulation the affinity constant is used. It is the inverted dissociation constant. so where [6] |
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 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
- ↑ 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
- ↑ Marín-Hernández A , Rodríguez-Enríquez S, Vital-González P A, et al. (2006). Determining and understanding the control of glycolysis in fast-growth tumor cells. Flux control by an over-expressed but strongly product-inhibited hexokinase. FEBS J., 273 , pp. 1975–1988(doi)
- ↑ 8.0 8.1 Dombrauckas, J. D., Santarsiero, B. D. & Mesecar, A. D. (2005) Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry 44, 9417–9429
- ↑ del Valle,P.,de Arriaga, D., Busto, F. and Soler, J. (1986) A study of the allosteric kinetics of Phycomyces pyruvate kinase as judged by the effect of e-alanine and fructose 1,6-bisphosphate. Biochim. Biophys. Acta 874, 193-204