Effect of trypsin microenvironment on the rate constants of elementary stages of the hydrolysis reaction of N
α-Benzoyl-L-arginine ethyl ester |
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Authors: | N L Zakharchenko E A Ermakova Yu F Zuev |
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Institution: | (1) Kazan Institute of Biochemistry and Biophysics, Kazan Scientific Center, Russian Academy of Sciences, ul Lobachevskogo 2/31, Kazan, 420111, Tatarstan, Russia |
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Abstract: | The hydrolysis reaction of N α-benzoyl-L-arginine ethyl ester catalyzed by trypsin from pig pancreas was comparatively studied in an aqueous buffer solution and in the system of reversed micelles of Aerosol OT in octane (pH 8.5) to determine the mechanisms of influence of the enzyme microenvironment on the rate constants of the elementary stages of the enzymatic reaction. The temperature dependences of the catalytic constant k cat and the rate constant of the second order k cat/K m (s, catalysis efficiency) allowed the determination of the rate constants and the activation energy of elementary stages of the enzymatic reaction. It was revealed that a decrease in the efficiency of catalytic action of trypsin in reverse micelles in comparison with an aqueous solution is first of all determined by a decrease in the rate constant of formation of the enzyme-substrate complex k 1. Possible mechanisms of the effect of the microenvironment on the elementary stages of catalytic action of the enzyme are discussed. |
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Keywords: | reverse micelles microenvironment trypsin |
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