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When a non-competitive inhibitor is added the Vmax is changed, while the Km remains unchanged. According to the Lineweaver-Burk plot the Vmax is reduced during the addition of a non-competitive inhibitor, which is shown in the plot by a change in both the slope and y-intercept when a non-competitive inhibitor is added. [8]
Effects of different types of inhibition on the double-reciprocal plot. When used for determining the type of enzyme inhibition, the Lineweaver–Burk plot can distinguish between competitive, pure non-competitive and uncompetitive inhibitors. The various modes of inhibition can be compared to the uninhibited reaction.
This can be competitive inhibition, uncompetitive inhibition, non-competitive inhibition or partially competitive inhibition. If the molecule induces enzymes that are responsible for its own metabolism, this is called auto-induction (or auto-inhibition if there is inhibition).
Uncompetitive inhibition (which Laidler and Bunting preferred to call anti-competitive inhibition, [1] but this term has not been widely adopted) is a type of inhibition in which the apparent values of the Michaelis–Menten parameters and are decreased in the same proportion.
Two equations listed below that are referred to as non-competitive substrate inhibition and competitive substrate inhibition models respectively by Shuler and Michael in Bioprocess Engineering: Basic Concepts. Note that the Haldane equation above is a special case of the following non-competitive substrate inhibition model, where KI >>Ks. [1]
Competitive inhibition can be overcome by adding more substrate to the reaction, which increases the chances of the enzyme and substrate binding. As a result, competitive inhibition alters only the K m, leaving the V max the same. [3] This can be demonstrated using enzyme kinetics plots such as the Michaelis–Menten or the Lineweaver-Burk plot.
If the ability of the inhibitor to bind the enzyme is exactly the same whether or not the enzyme has already bound the substrate, it is known as a non-competitive inhibitor. [1] [2] Non-competitive inhibition is sometimes thought of as a special case of mixed inhibition. In mixed inhibition, the inhibitor binds to an allosteric site, i.e. a ...
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