Question

A scientist discovers that a compound inhibits the action of an enzyme. What experiment can he perform to determine whether the compound is a competitive or noncompetitive inhibitor?

Answer 1

Answer:

The correct answer is "Raise the concentrations of the reactants to see if activity can be restored through reactant competition with the inhibitor for binding at the active site".

Explanation:

The missing options of this question are:

a) Raise the concentrations of the reactants to see if activity can be restored through reactant competition through the inhibitor for binding at the active site

b) Analyze the products of the enzyme-catalyzed reaction in the presence and absence of the inhibitor to see if the inhibitor changes their chemical composition.

c) Analyze the enzyme under conditions when the inhibitor is bound to see if the binding interaction between inhibitor and enzyme is covalent or noncovalent.

d) Raise the concentration of the inhibitor to see if it binds to more than one binding site on the enzyme

The correct answer is option a) "Raise the concentrations of the reactants to see if activity can be restored through reactant competition through the inhibitor for binding at the active site".

The most common way at which scientist determine whether a compound is a competitive or noncompetitive inhibitor is by raising the concentrations of the reactants to see if activity can be restored through reactant competition through the inhibitor for binding at the active site. A competitive inhibitor acts by binding to the active site of the enzyme, if the activity of the enzyme is restored by raising the concentration of the reactants, then the scientist can determine that the compound is a competitive inhibitor.

Answer 2

Answer

Raise the concentrations of the reactants to see if activity can be restored through reactant competition with the inhibitor for binding at the active site.

Explanation:

Competitive inhibitors have a structure similar to that of the normal substrate. Like the substrate, the inhibitor binds temporarily to the enzyme's active site but is not converted to products. This way, the inhibitor competes with the normal substrate for binding onto the enzyme's active site.

Non-competitive inhibitors do not compete with the normal substrate for the active site. They bind at a site different from the active site in a way that alters the structure of the active site. The result is that the normal substrate fails to bind to the active site.