Abstract
The aim of present study was to describe the graphical technique how to go from Hill concentration constant to Michaelis constant. To compare enzymatic processes, the kinetics of which is subjected to different regularities, it is possible to use constants that characterize catalytic activity (Vmax) and concentration constants that are the substrate concentration at which the rate of the enzymatic process is equal to a half of maximum permissible rate. Concentration constants are S0.5 for Hill equation and Km for Michaelis-Menton equation. The graphical approach was proposed in order to go from concentration constant of Hill equation to Michaelis concentration of the process that could be characterized by the same catalytic activity (the same values of minimum and maximum rates) similar to that observed in the process described by Hill equation.
Highlights
There exist enormous amounts of research findings on the activity of various enzymes
To find the constants for monomeric enzymes for which the dependence of the rate of a reaction, catalyzed by these enzymes, on substrate concentration is subjected to the hyperbolic kinetics [1,2,3], the Michaelis-Menten equation has to be used: V = Vmax·S/(Km + S), Where
V is the rate of a reaction catalyzed by the enzyme; S is a substrate concentration; Vmax is maximum rate of enzymatic reaction; Km is the Michaelis constant (Michaelis concentration), which is determined graphically as substrate (S) concentration at which V = 0.5Vmax and used for characterization of the affinity of the enzyme to a substrate
Summary
There exist enormous amounts of research findings on the activity of various enzymes. To find the constants for monomeric enzymes for which the dependence of the rate of a reaction, catalyzed by these enzymes, on substrate concentration is subjected to the hyperbolic kinetics [1,2,3], the Michaelis-Menten equation has to be used: V = Vmax·S/(Km + S), Where
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