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	Theoretical Analysis of the Relationship Between Positive/Negative Cooperativity and Enzyme Activation/Inhibition
	Ge, Hao ; Qian, Min
	2009
关键词	cooperativity enzyme activation/inhibition interaction
英文摘要	Cooperativity is one of the "paradigms" in enzyme kinetics and molecular biology. But the classical textbook treatment of enzyme kinetics always indeed separates the concepts of positive/negative cooperativity from enzyme activation/inhibition, at least partially. Few theoretical analysis of their relationship has been discussed, although its experimental investigations might date back at least to 1970s. In the present paper, we try to apply the change of free energy as a connective parameter for investigating the relationship between positive/negative cooperativity and enzyme activation/inhibition through several classic equilibrium binding models. It is explicitly shown that the terms of positive/negative cooperativity could be equivalently regarded as enzyme activation/inhibition of the saturation function induced by the substrate molecule itself rather than any other additional effectors. Moreover, both the degree of cooperativity phenomenon and the degree of enzyme activation/inhibition monotonically increase with the change of free energy. Note that this result is quite different from the idea of relating cooperativity to the concepts of "substrate activation/inhibition", which is identified when at high substrate concentrations the reaction rate decreases instead of tending towards the maximum velocity, since it always needs a second substrate molecule.; Mathematical & Computational Biology; SCI(E); 0; ARTICLE; 3; 204-213; 1
语种	英语
出处	SCI
出版者	interdisciplinary sciences computational life sciences
内容类型	其他
源URL	[http://hdl.handle.net/20.500.11897/247547]
专题	数学科学学院
推荐引用方式 GB/T 7714	Ge, Hao,Qian, Min. Theoretical Analysis of the Relationship Between Positive/Negative Cooperativity and Enzyme Activation/Inhibition. 2009-01-01.

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