Which statements about allosteric enzymes are true? exhibit cooperativity in substrate binding (homoallostery) exhibit regulation of their activity by other, effector molecules (heteroallostery) there is no difference in the binding curve for a cooperative binding versus noncooperative binding enzyme are frequently multisubunit proteins, with multiple active sites

The following statements are true:

Explanation:

The following statement is not true:

Yes there is a difference in the binding curve for a cooperative binding versus noncooperative binding.

For enzymes that show "positive substrate cooperativity" the binding of a substrate molecule to an active site increases the affinity of remaining active sites for more substrate.

While for enzymes that show "negative substrate cooperativity" the binding of a molecule of substrateto an active site decreases the affinity of the other active sites of the enzyme.

A, B y D are correct

The false statment  is: there is no difference in the binding curve for a cooperative binding versus noncooperative

Explanation:

Allosteric enzymes work by reversible binding with a small molecule of low molecular weight called an allosteric modulator or effector, that binding is non-covalent. If the modulator is the substrate it is called homoallosteric modulator if it is different it is called heteroallosteric modulator. When the allosteric activator binds to the allosteric site of the enzyme, it induces a conformational change that generates the active site making it accessible to the natural substrate of the enzyme. The binding of a substrate molecule to one of the enzyme subunits induces a conformational change in the neighbouring subunit facilitating the association of other substrate molecules and these changes are transmitted to the remaining subunits, therefore if there is a difference in the cooperative unions vs. non-cooperatives since each subunit has its own unique allosteric site.