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Findings from that experiment allowed for the divergence of non-competitive and competitive inhibition. Non-competitive inhibition affects the k cat value (but not the K m) on any given graph; this inhibitor binds to a site that has specificity for the certain molecule. Michaelis determined that when the inhibitor is bound, the enzyme would ...
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.
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.
Enzyme inhibition can refer to the inhibition of the expression of the enzyme by another molecule; interference at the enzyme-level, basically with how the enzyme works. This can be competitive inhibition, uncompetitive inhibition, non-competitive inhibition or partially competitive inhibition.
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]
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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.
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