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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.
The rate of reaction of many chemical reactions shows a linear response as function of the concentration of substrate molecules. Enzymes however display a saturation effect where,, as the substrate concentration is increased the reaction rate reaches a maximum value. Standard approaches to describing this behavior are based on models developed ...
Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions. Only a small proportion of enzyme-catalysed reactions have just one substrate, but the equation still often applies if only one substrate concentration is varied.
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.
Enzyme-substrate interactions align the reactive chemical groups and hold them close together in an optimal geometry, which increases the rate of the reaction. This reduces the entropy of the reactants and thus makes addition or transfer reactions less unfavorable, since a reduction in the overall entropy when two reactants become a single product.
Enzyme activity. An enzyme's name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in -ase. [1]: 8.1.3 Examples are lactase, alcohol dehydrogenase and DNA polymerase. Different enzymes that catalyze the same chemical reaction are called isozymes. [1]: 10.3
The rate of a reaction is the concentration of substrate disappearing (or product produced) per unit time (mol L −1 s −1). The % purity is 100% × (specific activity of enzyme sample / specific activity of pure enzyme). The impure sample has lower specific activity because some of the mass is not actually enzyme.