Answer:
(B) They may have binding sites for regulatory molecules that are separate from active sites.
(C) They generally have more than one subunit.
(E) They interconvert between a more active form and a less active form.
Explanation:
Allosteric enzymes are the regulatory enzymes that have a specific site for binding of modulator or effector molecule. The activity of these enzymes is altered by the noncovalent binding of modulators at the allosteric site. The binding of the modulator brings about a conformational change in the allosteric enzymes.
The relatively inactive conformation of these enzymes is called T state while the active conformation is the R state. Most of the allosteric enzymes have multiple subunits and deviate from Michaelis–Menten kinetics and exhibit a sigmoid saturation curve of V0 vs. [S].
The answer is <span>A. versatility</span>
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