Compare and contrast the actions of an allosteric effector, a competitive enzyme inhibitor, and a non-competitive inhibitor.

A chemical that binds to the active site of an enzyme and inhibits (prevents) a process by having a structure similar to that of the enzyme's substrate is known as a competitive inhibitor.

Competitive enzyme inhibitors slow down enzyme function and prevent the enzyme from catalyzing the process by acting at the active site and preventing substrate binding. By providing an extra substrate, the effect of a competitive inhibitor can be mitigated.

Non-competitive enzyme inhibitors work by interfering with substrate binding at a place other than the active site on the enzyme molecule.

Because the structure of the enzyme is permanently altered and the substrate will not attach to the active site, the effect of a non-competitive inhibitor cannot be undone by adding more substrate.

A conformational shift in the active site, which alters its shape and decreases the enzyme's affinity for its substrate, is known as an allosteric inhibitor. Allosteric effectors bind to enzymes to provide allosteric effects.

Allosteric effects that are positive lead the enzyme to be activated, which means that its activity is increased. Negative allosteric effects reduce the enzyme's activity by inhibiting it. Allosteric effectors attach to enzymes and cause them to go into an inactive state.