👁️‍🗨️ Watch the video to appreciate how the different metabolic pathways involving different enzymes can be regulated via feedback inhibition and allosteric regulation. 

Do note that the video focuses on allosteric inhibition. Enzyme whose activities are regulated by allosteric inhibitors, tend to catalyse the first reaction in a biochemical pathway. Thus the final product is able to switch off its own production as it builds up.

As seen in the figure, allosteric enzymes have multi-subunits. Each subunit has its own active site and allosteric site.

An allosteric enzyme activity can be altered by binding of regulatory molecules to an allosteric site or regulatory site.

Allosteric activators enable the binding of substrate to the active site and thus increase the rate of reaction. The enzyme will remain activated until the allosteric activator leaves the allosteric site.

Allosteric inhibitors prevent the binding of substrate to the active site and thus decreases the rate of reaction.

Another kind of allosteric activation is known as cooperativity.

Example: phosphofructokinase (PFK), exhibit cooperative binding, where one substrate molecule increases an enzyme affinity to additional substrate molecules and primes the enzyme to act on additional substrate molecules more readily leading to a sigmoidal activity curve.