When an allosteric enzyme is directly affected by a molecule that is not its substrate, this effect on the enzyme is called a heterotropic effect.
<h3>What is an allosteric enzyme?</h3>
Allosteric enzymes are catalysts that exhibit a site for binding that is distinct from the active site.
Allosteric enzymes are controlled by many effector compounds that can bind to different sites.
The active site of the enzyme is the molecular domain of this protein where reactants can bind during a chemical reaction.
The heterotropic effects occur when the ligands of allosteric modulators (effectors) are linked to the enzyme.
An allosteric modulator is a molecule that binds to the enzyme in a site different to the active site and this binding alters its tridimensional conformation, thereby activating it or deactivating it.
In conclusion, when an allosteric enzyme is directly affected by a molecule that is not its substrate, this effect on the enzyme is called a heterotropic effect.
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