By allosteric regulation an enzyme might be activated or inhibited. When a molecule regulates the activity of an enzyme by binding to a site outside of the active site, it is known as an allosteric molecule.
Allosteric regulation occurs when molecules bind to the enzyme on another side, which is not the binding site. This is the allosteric site, and molecules binding to these sites are the allosteric molecules.
Allosteric molecules can be either,
Allosteric inhibition is non-competitive inhibition because the allosteric molecule does not compete directly with the substrate.
It attaches to the enzyme at another site, impeding the substrate to bind the enzyme and turning off its function.
Allosteric activation is a cooperative process in which the enzyme function is enhanced. Some substrates can even work as allosteric activators for other active binding sites.
Allosteric enzymes can change their conformation, exhibiting active and inactive conformations as a result of substrate binding at the activated center and regulatory molecules at other binding sites -allosteric centers-.
According to this framework, When a molecule regulates the activity of an enzyme by binding to a site outside of the active site, it is known as an allosteric molecule.
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