You have added an irreversible inhibitor to a sample of enzyme and substrate. At this point, the reaction has stopped completely.

Question

What can you do to regain the activity of the enzyme?
View Available Hint(s)for Part B

Removing the irreversible inhibitor should get the reaction working again.
The enzyme is inactive at this point. New enzyme must be added to regain enzyme activity.
Adding more substrate will increase the rate of reaction.
Adding more inhibitor should get the reaction up to speed again.
Part C - Reversible inhibition
You have an enzymatic reaction proceeding at the optimum pH and optimum temperature. You add a competitive inhibitor to the reaction and notice that the reaction slows down.
What can you do to speed the reaction up again?
View Available Hint(s)for Part C

Add more inhibitor to speed up the reaction.
Add more substrate; it will outcompete the inhibitor and increase the reaction rate.
Increase the temperature.
Increase the pH.

Answer 1

Part B - Irreversible Inhibition

In the case of an irreversible inhibitor, once the inhibitor has bound to the enzyme, the enzyme cannot regain its activity simply through removal of the inhibitor. Therefore, the most appropriate action is:

• The enzyme is inactive at this point. New enzyme must be added to regain enzyme activity.

Part C - Reversible Inhibition

For a competitive inhibitor, the inhibitor competes with the substrate for binding to the active site of the enzyme. To counteract the effects of a competitive inhibitor and speed up the reaction, you can:

• Add more substrate; it will outcompete the inhibitor and increase the reaction rate.

Adding more substrate effectively increases the likelihood of substrate binding to the active site instead of the inhibitor, thereby enhancing the overall reaction rate.