ArticleMathematical biosciences2019
General mathematical formula for near equilibrium relaxation kinetics of basic enzyme reactions and its applications to find conformational selection steps.
Article in Mathematical biosciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
A general mathematical formula of basic enzyme reactions was derived with nearly no dependence on conditions nor assumptions on relaxation kinetic processes near equilibrium in a simple single-substrate-single-product enzyme reaction. The new formula gives precise relationships between the rate constants of the elementary reaction steps and the apparent relaxation rate constant, rather than the initial velocity that is generally used to determine enzymatic parameters according to the Michaelis-Menten theory. The present formula is shown to be complementary to the Michaelis-Menten formulae in a sense that the initial velocity and the relaxation rate constant data together could determine the enzyme-substrate dissociation constant K
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