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A theoretical study of optimization of generalized reversible three state kinetic scheme of enzymatic reaction with respect to the Maximum Entropy Production Principle (MEPP) is presented. We calculated entropy production for each reaction transition of the kinetic scheme as a function either of forward or backward rate constant. We found that for each transition a unique maximum in entropy production exists, and, therefore, the optimal value of the corresponding rate constant could be calculated. Following idea that only second order rate constants are not subjected to evolution1, optimal values of rate constants predicted by MEPP principle are compared to known experimentally determined values for three different types of the enzyme beta-lactamase: beta- lactamase I, PC1 beta-lactamase and RTEM beta-lactamase2. Our results show that MEPP could be an appropriate principle for evolutionary optimization of enzymatic reactions. [1] Heinrich, R., Schuster, S., Holzhutter, H.-G.Mathematical analysis of enzyme reaction systems using optimization principles (1991) European Journal of Biochemistry, 201, 1-21. [2] H. Christensen, M.T. Martin and G. Waley β-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism, (1990) Biochem. J. 266, 853-861.
maximum entropy production; enzymatic reactions; evolutionary optimization
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