Interdependence between cooperativity and control coefficients.
Influence of the concentration of internal metabolites on the control coefficient (defined as fractional change in flux per fractional change in enzyme activity) and regulatory properties of a given enzyme have been studied theoretically using a cyclic model of three enzymes. This model is useful to investigate the properties of the flux control coefficient for an enzyme following different rate equations. Enzymes can have high or low values of control coefficient irrespective of the type of kinetic equation, but the results obtained show that the sensitivity of these values to substrate variations is strongly dependent on its rate equation. These results help identify which kinetic equation allows the best control of a given metabolic pathway. These results have been applied to the purine nucleotide cycle. It is demonstrated that the best control of the cycle is reached when the irreversible reaction catalyzed by AMP deaminase follows a rate law that corresponds to a rational function of 2:2 degree with respect to AMP concentration.
Canela
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Department of Biochemistry and Physiology, Faculty of Chemistry, University of Barcelona, Catalonia, Spain.
Franco
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R
Cascante
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D000659:AMP Deaminase / Q000378:metabolism; D003198:Computer Simulation; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D009132:Muscles / Q000201:enzymology; D011685:Purine Nucleotides / Q000378:metabolism
D004798:Enzymes; D011685:Purine Nucleotides; D000659:AMP Deaminase