Abstract
Detailed kinetic analysis of the creatine kinase (CK) reaction catalyzed by soluble enzymes has been given many years ago1–3. However, it has already been known since 1975 that the behavior of CK in mitochondria under conditions of oxidative phosphorylation is not governed by substrate concentration in the medium and soluble enzyme kinetics, but even the direction of the CK reaction may be different depending on the oxidative phosphorylation, which very significantly increases the rate of phosphocreatine production and decreases the rate of the reverse reaction of ATP formation3.
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References
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Aliev, M.K., Saks, V.A. (1993). Mathematical Model of the Creatine Kinase Reaction Coupled to Adenine Nucleotide Translocation and Oxidative Phosphorylation. In: Schuster, S., Rigoulet, M., Ouhabi, R., Mazat, JP. (eds) Modern Trends in Biothermokinetics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2962-0_15
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