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Increasing the substrate concentration increases the rate of reaction (enzyme activity). However, enzyme saturation limits reaction rates. An enzyme is saturated when the active sites of all the molecules are occupied most of the time. At the saturation point, the reaction will not speed up, no matter how much additional substrate is added.
For a given enzyme concentration and for relatively low substrate concentrations, the reaction rate increases linearly with substrate concentration; the enzyme molecules are largely free to catalyse the reaction, and increasing substrate concentration means an increasing rate at which the enzyme and substrate molecules encounter one another.
In biochemistry, control coefficients [1] are used to describe how much influence a given reaction step has on the flux or concentration of the species at steady state.This can be accomplished experimentally by changing the expression level of a given enzyme and measuring the resulting changes in flux and metabolite levels.
Moreover, Kacser and Burns [13] suggested that since the flux–enzyme relationship is somewhat hyperbolic, and that for most enzymes, the wild-type diploid level of enzyme activity occurs where the curve is reaching a point in the curve where changes have little effect, then since a heterozygote of the wild-type with a null mutant will have ...
The enzyme unit, or international unit for enzyme (symbol U, sometimes also IU) is a unit of enzyme's catalytic activity. [1]1 U (μmol/min) is defined as the amount of the enzyme that catalyzes the conversion of one micro mole of substrate per minute under the specified conditions of the assay method.
in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA. Conservation of enzyme requires that [28] = where is now the total enzyme concentration. After combining the two expressions some straightforward algebra leads to the following expression for the concentration ...
where [A] is the fixed concentration of agonist and EC 50 is the concentration of agonist that results in half maximal activation of the receptor. Whereas the IC 50 value for a compound may vary between experiments depending on experimental conditions, (e.g. substrate and enzyme concentrations) the K i is an absolute value.
The katal (symbol: kat) is that catalytic activity that will raise the rate of conversion by one mole per second in a specified assay system. [1] It is a unit of the International System of Units (SI) [1] used for quantifying the catalytic activity of enzymes (that is, measuring the enzymatic activity level in enzyme catalysis) and other catalysts.