Allosteric effector is an enzyme activator or inhibitor that has its effect at a site other than the catalytic site of the enzyme. The effector can be described as an agent that facilitates a specific effect or an agent ... More »

Allosteric inhibition is the process by which a regulatory molecule binds to an enzyme in a spot different from the active site for another molecule. This causes a conformational change in the active site for the second ... More »

An allosteric regulation is the biochemical regulation of an enzyme or protein by the binding of an effector molecule to the protein's inactive, or allosteric, site. These effector molecules can enhance or inhibit the pr... More »

Allosteric control occurs when a small regulatory molecule causes the inhibition or activation of an enzyme at an allosteric site rather than the active site (the region of the enzyme that binds to substrates, where cata... More »

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The enzyme-substrate complex forms when a substrate binds to the active site of an enzyme, according to the University of California at Davis. The complex exists before the enzyme converts the substrate into a product. More »

The lock-and-key model refers to the way in which a substrate binds to an enzyme's active site. Similar to how a key has to be the correct one for a lock, no reaction takes place if an incorrect substrate tries to bind. More »

ATP synthase is an enzyme that plays a vital role in the addition of a phosphate to ADP, or adenosine diphosphate, to form ATP, or adenosine triphosphate. The enzyme is located within the mitochondria of a cell, where th... More »