What are characteristics of allosteric enzymes?
O They may have binding sites for regulatory molecules that are separate from active sites.
O They interconvert between a more active form and a less active form.
O They generally have more than one subunit.
O They conform to Michaelis–Menten kinetics.
O They tend to have a hyperbolic curve of V 0 V0 vs. [S].
They may have binding sites for regulatory molecules that are separate from active sites.
Allosteric enzymes has allosteric sites where the regulatory molecule is joined. When it happens the enzyme change their shape which results in an apparent change in binding affinity at a different ligand binding site or change how enzyme works.
