Join thousands of students who trust us to help them ace their exams!Watch the first video
Multiple Choice
The binding of an allosteric inhibitor to an enzyme causes the rate of product formation by the enzyme to decrease. Which of the following best explains why this decrease occurs?
A
The allosteric inhibitor binds to the active site, preventing the substrate from binding.
B
The allosteric inhibitor causes free energy change of the reaction to increase.
C
The allosteric inhibitor lowers the temperature of the active site.
D
The allosteric inhibitor binds to the substrate and prevents it from binding at the active site.
E
The allosteric inhibitor causes a structural change in the enzyme that prevents the substrate from binding at the active site.
Verified step by step guidance
1
Understand the concept of allosteric inhibition: Allosteric inhibitors bind to a site on the enzyme other than the active site, known as the allosteric site. This binding causes a conformational change in the enzyme's structure.
Recognize the effect of the conformational change: The structural change in the enzyme alters the shape of the active site, which can prevent the substrate from binding effectively.
Eliminate incorrect options: The allosteric inhibitor does not bind to the active site directly, so it does not prevent substrate binding by occupying the active site itself.
Consider the energy and temperature options: Allosteric inhibitors do not typically change the free energy of the reaction or the temperature of the active site. These options are not relevant to the mechanism of allosteric inhibition.
Identify the correct explanation: The correct explanation is that the allosteric inhibitor causes a structural change in the enzyme that prevents the substrate from binding at the active site, thereby decreasing the rate of product formation.