期刊
JOURNAL OF CHEMICAL PHYSICS
卷 136, 期 5, 页码 -出版社
AMER INST PHYSICS
DOI: 10.1063/1.3681942
关键词
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资金
- TAMOP [4.2.1/B-09/1/KONV-2010-0007]
- European Union
- European Social Fund
The Michaelis-Menten mechanism is an extremely important tool for understanding enzyme-catalyzed transformation of substrates into final products. In this work, a computationally viable, full stochastic description of the Michaelis-Menten kinetic scheme is introduced based on a stochastic equivalent of the steady-state assumption. The full solution derived is free of restrictions on amounts of substance or parameter values and is used to create stochastic maps of the Michaelis-Menten mechanism, which show the regions in the parameter space of the scheme where the use of the stochastic kinetic approach is inevitable. The stochastic aspects of recently published examples of single-enzyme kinetic studies are analyzed using these maps. (C) 2012 American Institute of Physics. [doi:10.1063/1.3681942]
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