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From the
1 From the Department of Biochemistry, Australian National University, The John Curtin School of Medical Research, Canberra, Australia, and the Department of Biochemistry, University of Wisconsin, Madison, Wisconsin
The mechanism of the reaction catalyzed by adenosine triphosphate: creatine phosphotransferase has been studied by measuring the initial velocities of the exchange with isotopically labeled substrates.
The rates of the creatine-phosphocreatine, ATP-ADP, and ADP-ATP exchanges at equilibrium are approximately equal and dependent on the concentrations of Mg2+ and ADP3-.
The ADP-ATP exchange rate increases hyperbolically to a maximum value as the concentration of the creatine-phosphocreatine pair is raised while the creatine-phosphocreatine exchange rate increases initially and then decreases with increasing concentrations of the MgATP-MgADP pair. The decrease in the exchange rate was shown to be due to the inhibitory effect of NaCl which is introduced when the reactants are formed from MgCl2 and the sodium salts of the nucleotides.
The formation of a dead end enzyme-MgADP-creatine complex has been confirmed, but the experimental data were not in accord with the formation of a dead end enzyme-MgATP-phosphocreatine complex.
These data confirm the results from initial velocity and product inhibition studies which indicate that the mechanism of the reaction is rapid equilibrium, random.
Submitted on August 16, 1965
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