What is the function of molecules that change the shape and activity of an enzyme by binding at a site on the enzyme?

Molecules that bind to an enzyme at a site other than the active site and cause a change in the enzyme's shape and activity are known as allosteric regulators. These molecules can either enhance or inhibit the enzyme's function. When an allosteric regulator binds, it induces a conformational change in the enzyme, which can either increase or decrease its affinity for substrates or alter its catalytic activity. This mechanism provides a means of fine-tuning metabolic pathways, allowing the regulation of enzyme activity in response to changes in the cellular environment or the needs of the organism.

Other choices represent different roles: enzyme inhibitors typically block the activity of enzymes by binding to the active site or another site, but not in a way that is specifically defined as allosteric regulation. Cofactors are non-protein molecules that assist enzymes in catalyzing reactions but do not alter the enzyme's shape. Hormones serve as signaling molecules in the body and do not directly interact with enzyme activity in this context. Thus, allosteric regulators specifically relate to the modulation of enzyme function through binding at distinct sites.