On the Minimal Model of Kinetic Cooperativity
DOI:
https://doi.org/10.15407/ujpe68.10.684Keywords:
monomeric enzymes, kinetic cooperativity, conformational regulation, nonMichaelis schemes, kinetic resonance, glucokinaseAbstract
The minimal 3-state scheme of kinetic cooperativity of monomeric enzymes is subjected to a detailed analysis. The rigorous criteria of the positive cooperativity and its sigmoidal version are established in terms of the system parameters (rate constants). It is shown that the cooperativity extent is especially sensitive to the rates and direction of the exchange between conformational states of the free enzyme. However, no necessity of the “kinetic resonance” (or, moreover, its generality claimed recently) for enhancing the cooperativity is revealed. Overall, while the minimal 3-state model serves well for the qualitative understanding of the origin of kinetic cooperativity, it is hardly suitable for the quantitative description of reactions of real enzymes, as it is shown with the case of glucokinase.
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