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You have isolated a previously unstudied protein, identified its complete structure in detail, and determined that it catalyzes the breakdown of a large substrate. You notice it has two binding sites. One of these is large, apparently the bonding site for the large substrate; the other is small, possibly a binding site for a regulatory molecule. What do these findings tell you about the mechanism of this protein?

1 It is probably a cell membrane transport protein–like an ion channel.
2 It is probably a structural protein that is involved in cell-to-cell adhesion.
3 It is probably an enzyme that works through allosteric regulation.
4 It is probably an enzyme that works through competitive inhibition.
5 It is probably a structural protein found in cartilage or skeletal tissue.

Answer :

lucasolvfranco

Answer:

3. It is probably an enzyme that works through allosteric regulation.

Explanation:

Allosteric regulation is any form of regulation in which a regulatory molecule (inhibitory or activating) binds to an enzyme at a different site than the common active site, this place is called an allosteric site.

These enzymes are part of some of our metabolic regulators and are known as allosteric enzymes. This type of enzyme has multiple active sites, located in several protein subunits.

When an allosteric inhibitor binds to an enzyme, all active sites change in ways that reduce its activity, while an allosteric activator enhances the functions of the active sites by binding to the enzyme.

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