An Allosteric Enzyme Differs from a Michaelis-Menten Enzyme Because the Allosteric

An allosteric enzyme differs from a Michaelis-Menten enzyme because the allosteric enzyme

A) has a more active binding site that is more polar and will hold the substrate longer.
B) displays cooperativity in which the binding of a substrate to the active site on one subunit affects the binding of substrate at other subunits.
C) operates to change reaction rates of all of the stereoisomers of a compound, not just one.
D) will catalyze all the reactions of a substance produced in a series of steps.