The binding of a compound to an enzyme is observed to slow down or stop the rate of the reaction catalyzed by the enzyme. increasing the substrate concentration reduces the inhibitory effects of this compound. which of the following could account for this observation?

a)the compound reduces disulfide bonds, causing the enzyme molecules to partially unfold.
b)the compound causes a cofactor to be lost from the enzyme.
c)the compound forms a covalent bond with one of the amino acid residues needed for enzyme activity.
d)the compound is a negative allosteric regulator.
e)the compound is a competitive inhibitor.

The correct answer is option e) "The compound is a competitive inhibitor".

Explanation:

A competitive inhibitor is a compound that resembles the normal substrate of an enzyme, resulting in the enzyme binding to the inhibitor and preventing that the enzyme catalyzes the reaction. The effect of the inhibitor is to slow down or stop the rate of the reaction catalyzed by the enzyme. Usually the action of this type of inhibitor is reduced by an increase in the substrate's concentration. Therefore, the compound described in the question belongs to a competitive inhibitor.

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