Join thousands of students who trust us to help them ace their exams!Watch the first video
Multiple Choice
Which of the following statements is false regarding inhibitors & enzyme-catalyzed reactions?
A
The Vmax of an enzyme-catalyzed reaction will never increase in the presence of an enzyme-inhibitor.
B
Enzyme inhibitors can be secreted via exocytosis to defend against harmful threats.
C
At saturating [S], the rate is directly proportional to [enzyme].
D
The EA for catalyzed & uncatalyzed reactions are equal, but the Keq is more favorable in a catalyzed reaction.
E
Binding of an inhibitor to an enzyme can be reversible or irreversible.
Verified step by step guidance
1
Understand the role of enzyme inhibitors: Enzyme inhibitors are molecules that decrease the activity of enzymes. They can bind to enzymes and reduce their activity, either reversibly or irreversibly.
Review the concept of Vmax: Vmax is the maximum rate of an enzyme-catalyzed reaction when the enzyme is saturated with substrate. In the presence of an inhibitor, Vmax can decrease, but it will not increase.
Consider the effect of substrate concentration: At saturating substrate concentrations, the reaction rate is directly proportional to the enzyme concentration, as all enzyme active sites are occupied by the substrate.
Examine the statement about activation energy (EA) and equilibrium constant (Keq): The activation energy for catalyzed reactions is lower than for uncatalyzed reactions, which increases the reaction rate. However, the equilibrium constant (Keq) is not affected by the presence of a catalyst; it remains the same for both catalyzed and uncatalyzed reactions.
Evaluate the secretion of enzyme inhibitors: Enzyme inhibitors can indeed be secreted by cells via exocytosis as a defense mechanism against harmful threats, such as pathogens or toxins.