allosterický

Allosteric refers to a type of regulation in which a molecule binds to a site other than the active site of an enzyme or protein, causing a conformational change that affects the function of the molecule. This regulatory mechanism is crucial in various biological processes, allowing for fine-tuned control of enzyme activity and protein function. The allosteric site is typically located at a distance from the active site, and the binding of an allosteric effector can either activate or inhibit the enzyme or protein. Allosteric regulation is common in many proteins, including hemoglobin, where oxygen binding at one site affects the affinity of other sites for oxygen. This type of regulation is distinct from competitive inhibition, where the inhibitor binds directly to the active site, and from noncompetitive inhibition, where the inhibitor binds to a site other than the active site but does not cause a conformational change. Allosteric regulation plays a vital role in maintaining homeostasis and ensuring the proper functioning of biological systems.