Characterization of the complete three-dimensional structure of a newly purified protein suggests that it catalyzes the breakdown of a large substrate. The protein consists of a single polypeptide chain. It has a large pocket that appears to be the binding site for the substrate and a smaller indentation that appears to be the binding site for a regulatory molecule. What do these structural observations suggest about the mechanism by which the activity of this protein is likely regulated? Choices:A) It is probably an enzyme that is regulated by noncompetitive inhibition. B) It is probably a multi-subunit enzyme that is regulated by allosteric regulation. C) It is probably an enzyme that is regulated by competitive inhibition. D) It is probably an enzyme that is regulated by cooperativity.

Question

Biology

Leticia Key

11 June, 23:26

Characterization of the complete three-dimensional structure of a newly purified protein suggests that it catalyzes the breakdown of a large substrate. The protein consists of a single polypeptide chain. It has a large pocket that appears to be the binding site for the substrate and a smaller indentation that appears to be the binding site for a regulatory molecule. What do these structural observations suggest about the mechanism by which the activity of this protein is likely regulated? Choices:A) It is probably an enzyme that is regulated by noncompetitive inhibition. B) It is probably a multi-subunit enzyme that is regulated by allosteric regulation. C) It is probably an enzyme that is regulated by competitive inhibition. D) It is probably an enzyme that is regulated by cooperativity.

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Makhi · Answer 1

A) It is probably an ezyme that is regulated by noncompetitive inhibition.

Explanation:

This protein is an enzyme that consists of a single polypeptide chain, this means that it doesn't have more subunits. The pocket is in the binding site for substrate or active site, and the indentation is a binding site for another molecule. This different molecule is a regulatory molecule or an inhibitor. In this scenario, the inhibitor binds to another site that is not the active site. When an inhibitor binds to a site away from the active site, it is said that this molecule acts as a noncompetitive inhibitor.