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  • Title: Henri-Michaelis-Menten kinetics of reversible enzymic reactions, and the determination of rate constants from kinetic constants.
    Author: Barnsley EA.
    Journal: Sci Prog; 2022; 105(2):368504221100027. PubMed ID: 35549765.
    Abstract:
    The Michaelis constants derived for two reversible uni-reactant - uni-product reaction models, given originally by Haldane, are corrected. In the direction starting with the reactant having the lower binding constant, the steady state is one in which the enzyme-reactant intermediate has a concentration approximating the final equilibrium concentration., Consequently, the Haldane relationship is generally invalid, and kinetic analyses to validate the use of the kinetic constant ratio (kcat/Km) as a measure of specificity are also generally invalid. This correction of Michaelis constants is pertinent to attempts to back calculate rate constants from experimental values: the Michaelis constant used must be correct.
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