Allosteric inhibitors refer to molecules that bind to the enzyme at a site other than the active site, known as the allosteric site, leading to a conformational change in the enzyme and reducing its activity[1]. This type of inhibition is known as allosteric inhibition and is a form of noncompetitive inhibition[1][5].
When an allosteric inhibitor binds to the enzyme, it induces a change in the enzyme’s three-dimensional shape, which can negatively impact its catalytic activity[1]. Allosteric inhibitors can regulate enzyme activity by modulating the binding affinity of substrates or cofactors, or by interfering with the enzyme’s catalytic turnover rate[1][3].
The concept of allosteric regulation is a fundamental aspect of enzyme control in cellular processes. Allosteric regulation involves a natural control mechanism where various effectors can act as allosteric activators, enhancing the enzyme’s activity, or as allosteric inhibitors, decreasing the enzyme’s activity[2]. These effectors can be other molecules or ions that bind to the enzyme at specific allosteric sites[2].
The use of allosteric inhibitors has gained significant attention in drug discovery research. By targeting specific allosteric binding sites, researchers can modulate protein function and achieve therapeutic effects. Allosteric inhibitors offer potential advantages such as increased selectivity, reduced side effects, and the ability to target proteins with challenging or highly conserved active sites[3][4].
Overall, allosteric inhibitors are molecules that bind to enzyme allosteric sites, leading to changes in enzyme conformation and regulation of enzyme activity. They play a critical role in drug discovery and can offer advantages in terms of selectivity and targetability.
Sources:
Allosteric Inhibition – The Definitive Guide | Biology Dictionary
1.18: Enzymes and Allosteric Regulation – Biology LibreTexts
Enzyme regulation (article) | Khan Academy
Allosteric regulation – Wikipedia
Allosteric inhibition explained through conformational ensembles …
