allosteric inhibition
inhibition by a binding event at a site different from the active site, which induces a conformational change and reduces the enzyme’s affinity for its substrate
Allosteric inhibition is a type of enzyme inhibition in which an inhibitor molecule binds to a site on the enzyme molecule that is distinct from the active site. This results in a conformational change in the enzyme that affects its ability to bind to and catalyze its substrate(s).
In other words, allosteric inhibition involves the binding of a molecule to a specific site on the enzyme that is not involved in the catalytic activity of the enzyme. This binding causes a change in the shape of the enzyme, which can either decrease its affinity for its substrate or prevent it from catalyzing the reaction altogether.
Allosteric inhibitors can be either reversible or irreversible. Reversible inhibitors bind to the enzyme with relatively weak interactions and can be removed from the enzyme under certain conditions, while irreversible inhibitors bind to the enzyme with high affinity and permanently inhibit its activity.
Allosteric inhibition is a mechanism of regulation used by cells to control enzymatic activity. By inhibiting the activity of an enzyme through allosteric regulation, cells can prevent the buildup of toxic intermediates or control metabolic pathways.
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