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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.
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.
Enzymes can be classified by two main criteria: either amino acid sequence similarity (and thus evolutionary relationship) or enzymatic activity. Enzyme activity. An enzyme's name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in -ase.
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 ...
The flux control coefficient, instead, measures how much influence a given step has on the steady-state flux. A step with a high flux control coefficient means that changing the activity of the step (by changing the expression level of the enzyme) will have a large effect on the steady-state flux through the pathway and vice versa.
Several factors affect the activity of enzymes (and other catalysts) including temperature, pH, the concentration of enzymes, substrate, and products. A particularly important reagent in enzymatic reactions is water, which is the product of many bond-forming reactions and a reactant in many bond-breaking processes.
Michaelis–Menten plot of the reaction velocity (v) against substrate concentration [S] of normal enzyme activity (1) compared to enzyme activity with a competitive inhibitor (2). Adding a competitive inhibitor to an enzymatic reaction increases the K m of the reaction, but the V max remains the same.
The activity of the enzyme catalysing the reaction; The properties of the enzyme; The metabolite concentration affecting enzyme activity. [5] Considering the above, the metabolic fluxes can be described as the ultimate representation of the cellular phenotype when expressed under certain conditions.