Michaelis-Menten mechanism for single-enzyme and multi-enzyme system under stochastic noise and spatial diffusion |
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Authors: | Ming Yi Quan Liu |
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Institution: | a Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan 430071, China b College of Basic Sciences, Huazhong Agriculture University, Wuhan 430071, China |
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Abstract: | The investigation of enzymatic reaction under stochastic effect and spatial effect is an interesting problem. By virtue of Monte Carlo simulation, the stochastic dynamic of enzyme and the related Michaelis-Menten mechanism with stochastic internal noise and spatial diffusion are explored in this article. (i) For the single-enzyme system, two cases, including the fast phosphorylation case X. S. Xie, et al., J. Phys. Chem. B 109 (2005) 19068] and slow phosphorylation case X. S. Xie, et al., Nat. Chem. Biol. 2 (2006) 87] are considered. It is found the micro enzymatic velocity rate shows a rough hyperbolic dependence on the substrate concentration, hence obeys the Michaelis-Menten law qualitatively. In addition, our result reveals that diffusion rate can adjust the Michaelis-Menten curve; especially, it is shown that increasing diffusion rate enhances the micro enzyme rate. (ii) For the multi-enzyme system, a typical example, i.e., MAPK signaling pathway is used. We apply the Michaelis-Menten mechanism to the MAPK cascade and give a simple comparison for the signaling ability between the Michaelis-Menten mechanism and the single collision mechanism J. W. Locasale et al., PLOS Comput. Biol. 4 (2008) e1000099]. |
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Keywords: | Stochastic noise Spatial diffusion Single enzyme Michaelis-Menten mechanism MAPK cascade |
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