Difference between revisions of "Pyruvate kinase"
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|<math>Ka_{SER}</math> | |<math>Ka_{SER}</math> | ||
|5 mM | |5 mM | ||
− | | For allosteric regulation the affinity constant is used. It is the inverted dissociation constant. so <math> Ka_{SER} = \frac{1}{K_d} where <math> k_d = 0.2 mM</math> | + | | 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> |
|} | |} | ||
Revision as of 17:29, 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
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 |
---|---|---|---|
3 | HeLa cell line | ||
195172 | Recalculated from the ΔGº´ = - 31.4 KJ mol-1. | ||
0.014 | |||
0.4 | |||
10 | |||
0.86 | |||
2.5 | |||
1 | |||
5 mM | For allosteric regulation the affinity constant is used. It is the inverted dissociation constant. so where |