What is the term for a change at a location on a protein that affects its activity but is not at the active site?

The term that describes a change at a location on a protein that affects its activity without being at the active site is known as allosteric regulation. Allosteric regulation refers to the process by which the binding of a molecule at a specific site on a protein, known as the allosteric site, leads to a conformational change in the protein. This alteration in shape can enhance or inhibit the protein's activity, despite the active site being unaffected directly by the binding event.

In the context of enzymes, allosteric sites are distinct from the active site where substrate molecules bind. When an allosteric effector (which can be an activator or inhibitor) binds to this site, it can modify the enzyme's conformation, thereby altering its catalytic efficiency or altering the affinity for the substrate at the active site.

Covalent modification refers to the permanent alteration of a protein through the formation of covalent bonds, typically associated with enzymes, while competitive inhibition involves the competition between a substrate and an inhibitor for binding to the active site. Substrate binding is simply the initial interaction that occurs between an enzyme and its substrate at the active site. In contrast, allosteric regulation involves non-active-site interactions that fine-tune the protein's function