Question
Researchers investigated the influence of environmental pH on the activity of peroxidase, an enzyme that catalyzes the conversion of hydrogen peroxide to water and oxygen gas. In an experiment, the researchers added a hydrogen peroxide solution containing guaiacol to several identical test tubes and adjusted the solution in each test tube to a different pH. The researchers included the guaiacol because it caused the solutions to change color as the reactions proceeded, which the researchers relied on for measuring reaction rates. Finally, the researchers added the same amount of peroxidase to each test tube and measured the rate of each reaction at 23°C
. The results of the experiment are represented in Figure 1.

▶️Answer/Explanation
Ans: A
Based on Figure 1, peroxidase’s optimal pH is 5. A change from a moderately acidic environment (pH near 6) to a basic environment (pH above 7) will result in a decrease in peroxidase activity.
Question
Researchers investigated the effect of urea on the three-dimensional structure of a certain enzyme. The researchers dissolved the enzyme in an aqueous buffer solution and added urea to the solution. The enzyme did not appear to have a secondary or tertiary structure. The researchers carefully removed the urea from the solution and determined that the enzyme had the original secondary and tertiary structure again.
Based on the results of the experiment, which of the following statements best predicts the effect of urea on the enzyme’s function?
A. Function will be disrupted by adding the urea and regained by removing the urea.
B. Function will be disrupted by adding the urea, but it will not be regained by removing the urea.
C. Function will be gained by adding the urea and disrupted by removing the urea.
D. Function will be unaffected by the addition and removal of the urea.
▶️Answer/Explanation
Ans: A
Based on the information, adding the urea denatures the enzyme, which will disrupt the enzyme’s function by disrupting the active site. In contrast, removing the urea causes the enzyme to refold, which will restore the active site and the enzyme’s function.
Question
In an experiment, a researcher prepares a reaction mixture by dissolving a substance in a buffered solution. The substance is the substrate of a certain enzyme. The researcher adds a small amount of the enzyme to the reaction mixture and measures the amount of product that is formed over time. The data are represented in Figure 1.

Figure 1. The amount of product formed by an enzyme-catalyzed reaction over time
Which of the following best predicts the immediate result of adding more substrate to the reaction mixture at the point indicated by the arrow in Figure 1?
A. The amount of product will decrease until the reaction rate goes to zero.
B. The amount of product will decrease until the reaction reaches its equilibrium point or until the enzyme is been used up by the reaction.
C. The amount of product will increase until the reaction reaches its equilibrium point or until the substrate is used up by the reaction.
D. The amount of product will increase without stopping because the enzyme will be unchanged by the reaction.
▶️Answer/Explanation
Ans: C
The graph shown in Figure 1 indicates that the amount of product became constant as a consequence of the reaction reaching its equilibrium point or as a consequence of the substrate being used up. Adding more substrate will likely result in an increase in the amount of product because the reaction catalyzed by the enzyme will convert the added substrate into product.
Question
Alcohol dehydrogenase (ADH) is an enzyme that aids in the decomposition of ethyl alcohol (\(C_2H_5OH\)) into nontoxic substances. Methyl alcohol acts as a competitive inhibitor of ethyl alcohol by competing for the same active site on ADH. When attached to ADH, methyl alcohol is converted to formaldehyde, which is toxic in the body.
Which of the following statements best predicts the effect of increasing the concentration of substrate (ethyl alcohol), while keeping the concentration of the inhibitor (methyl alcohol) constant?
A. There will be an increase in formaldehyde because ADH activity increases.
B. Competitive inhibition will be terminated because ethyl alcohol will bind to methyl alcohol and decrease ADH activity.
C. The peptide bonds in the active site of the enzyme will be denatured, inhibiting the enzyme.
D. Competitive inhibition will decrease because the proportion of the active sites occupied by substrate will increase.
▶️Answer/Explanation
Ans: D
The increase in amount of substrate will increase the number of enzyme-ethanol complexes formed, increasing the amount of nontoxic product formed from ethyl alcohol.