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Mixed inhibition
From Wikipedia, the free encyclopedia
Mixed inhibition refers to a combination of two different types of reversible enzyme inhibition--competitive inhibition and uncompetitive inhibition. The term 'mixed' is used when the inhibitor can bind to either the free enzyme or the enzyme-substrate complex. In mixed inhibition, the inhibitor binds to a site different from the active site where the substrate binds.
Mathematically, mixed inhibition occurs when the alpha and alpha-prime factors (introduced into the Michaelis-Menten equation to account for competitive and uncompetitive inhibition, respectively) are both present (i.e., greater than unity).
In a special case of mixed inhibition, the alpha and alpha-prime factors are equal, and noncompetitive inhibition occurs.
With this type of inhibition Km decreases and Vmax decreases.
Competitive inhibition - Uncompetitive inhibition - Non-competitive inhibition - Suicide inhibition - Mixed inhibition
Acetylcholinesterase inhibitors - Aromatase inhibitors - Carbonic anhydrase inhibitors - Kinase inhibitors - Monoamine oxidase inhibitors - Reverse transcriptase inhibitors - Phosphodiesterase inhibitors - Protease inhibitors
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