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Allosteric enzymes are enzymes with multiple binding sites that can be activated by a molecule. In allosteric enzymes, the binding of a regulatory molecule at one site affects the enzyme's activity at another site. This allows for the regulation of enzyme activity in response to the presence of specific molecules.

Competitive and non-competitive enzymes are terms used to describe the inhibition of enzyme activity by molecules that either compete with the substrate for the active site (competitive) or bind to a different site on the enzyme, altering its shape and activity (non-competitive).

Cooperative enzymes refer to enzymes that have multiple subunits that interact with one another, influencing each other's activity. This can result in positive cooperativity, where the binding of one substrate molecule enhances the binding of subsequent substrate molecules, or negative cooperativity, where the binding of one substrate molecule inhibits the binding of subsequent substrate molecules.