2015/01/10 by Vahe Galstyan, Galstyan, Vahe
Physics and Astronomy · #92C45 #Chemical Physics (physics.chem-ph) #FOS: Physical sciences #msc:92C45 #physics.chem-ph
paper · pdf · doi:10.48550/arxiv.1501.02392
4 pages, 3 figures
arxiv created 2015/01/10 · arxiv updated 2015/01/13
In biochemical systems the Michaelis-Menten (MM) scheme is one of the best-known models of the enzyme- catalyzed kinetics. In the academic literature the MM approximation has been thoroughly studied in the context of differential equation models. At the level of the cell, however, molecular fluctuations have many important consequences, and thus, a stochastic investigation of the MM scheme is often necessary. In their work Barik et al. [Biophysical Journal, 95, 3563-3574, (2008)] presented a stochastic approximation of the MM scheme. They suggested a substitution of the propensity function in the reduced master equation with the total quasi-steady- state approximation (tQSSA) rate. The justification of the substitution, however, was provided for a special case only and did not cover the whole parameter domain of the tQSSA. In this manuscript we present a derivation of the stochastic tQSSA that is valid for the entire tQSSA parameter domain.