Monte Carlo simulations of single- and multistep enzyme-catalyzed reaction sequences: effects of diffusion, cell size, enzyme fluctuations, colocalization, and segregation

The Journal of Chemical Physics
James B AndersonJörg Kussmann

Abstract

Following the discovery of slow fluctuations in the catalytic activity of an enzyme in single-molecule experiments, it has been shown that the classical Michaelis-Menten (MM) equation relating the average enzymatic velocity and the substrate concentration may hold even for slowly fluctuating enzymes. In many cases, the average velocity is that given by the MM equation with time-averaged values of the fluctuating rate constants and the effect of enzyme fluctuations is simply averaged out. The situation is quite different for a sequence of reactions. For colocalization of a pair of enzymes in a sequence to be effective in promoting reaction, the second must be active when the first is active or soon after. If the enzymes are slowly varying and only rarely active, the product of the first reaction may diffuse away before the second enzyme is active, and colocalization may have little value. Even for single-step reactions the interplay of reaction and diffusion with enzyme fluctuations leads to added complexities, but for multistep reactions the interplay of reaction and diffusion, cell size, compartmentalization, enzyme fluctuations, colocalization, and segregation is far more complex than for single-step reactions. In this paper,...Continue Reading

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Citations

Aug 21, 2012·Biophysical Chemistry·Vladimir P Zhdanov, Fredrik Höök
Sep 23, 2014·Molecular Microbiology·Jacek T MikaBert Poolman
Mar 19, 2015·European Biophysics Journal : EBJ·Vladimir P Zhdanov, Fredrik Höök
Mar 31, 2018·The European Journal of Neuroscience·Kim T BlackwellDavid M Lovinger
Sep 14, 2017·The Journal of Physical Chemistry. B·C Weistuch, S Pressé

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