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The accuracy of rapid equilibrium assumption in steady-state enzyme kinetics is a function of equilibrium segment structure and properties

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Abstract

Quantitative evaluation of the accuracy of the rapid equilibrium assumption in steady-state enzyme kinetics was obtained for an arbitrary mechanism of an enzymatic reaction. This evaluation depends only on the structure and properties of an equilibrium segment; it is independent on the structure and properties of the remaining part (stationary) of the kinetic scheme. In the rapid equilibrium assumption, the smaller the values are of the edges that leave the equilibrium segment in relation to the values of the edges within the equilibrium segment, the higher the accuracy of determination of the reaction velocity is, as well as the concentrations of intermediates.

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Authors and Affiliations

  1. International Biotechnological Center and Faculty of Bioengineering and Bioinformatics, Moscow State University, Moscow, 119991, Russia

    P. V. Vrzheshch

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  1. P. V. Vrzheshch
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Correspondence to P. V. Vrzheshch.

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Original Russian Text © P.V. Vrzheshch, 2015, published in Biofizika, 2015, Vol. 60, No. 2, pp. 262–269.

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Vrzheshch, P.V. The accuracy of rapid equilibrium assumption in steady-state enzyme kinetics is a function of equilibrium segment structure and properties. BIOPHYSICS 60, 205–211 (2015). https://doi.org/10.1134/S0006350915020219

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  • DOI: https://doi.org/10.1134/S0006350915020219

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