Biochemistry Questions Biochemistry Questions / Discuss the role of allosteric modulators in enzyme activity regulation. How do allosteric modulators differ from competitive inhibitors in terms of binding sites and effects on enzyme function?

Allosteric modulators, sometimes called non-competitive inhibitors, are regulatory molecules able to change the activity of an enzyme. These molecules bind to allosteric sites on the target enzyme, causing a structural alteration preventing the normal catalytic process from occurring.

Although allosteric modulators can increase enzyme activity, they are typically used to suppress it.

Due to the binding of an allosteric modulator being independent from the orthosteric (active) site, the activity of these molecules is independent of the substrate concentration. This can allow for lower doses to be administered to patients, and decrease the frequency of administration.