Pyruvate kinase
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 | Organism | Remarks |
---|---|---|---|
0.06 [2] | HeLa cell line | ||
651[3] | |||
0.1[4] | |||
1.1[4] | |||
[4] | |||
3.5[4] |
Alternative parameter values
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)
- ↑ 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)
- ↑ Arbitrary value
- ↑ 4.0 4.1 4.2 4.3 Cite error: Invalid
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