Henri-Michaelis-Menten kinetics of reversible enzymic reactions, and the determination of rate constants from kinetic constants
Year: 2022
Type: article
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.
Source: Science Progress
Author: Eric A. Barnsley
Language: English
Subfield: Organic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $2,100
OpenAlex ID: W4280504841