18 Questions
What type of enzyme inhibition occurs when the inhibitor binds to a different part of the enzyme, changing its shape and decreasing the reaction rate?
Non-competitive inhibition
Which type of inhibition occurs when the end product of a reaction binds to the enzyme at the start of the pathway, stopping the pathway until the end product concentration decreases?
Feedback inhibition
What is the key difference between competitive and non-competitive inhibition?
Competitive inhibitors bind to the active site, while non-competitive inhibitors bind elsewhere on the enzyme.
What is the main advantage of immobilizing enzymes in alginate?
It allows the enzyme to be reused and the reaction to flow continuously.
How does the Michaelis-Menten equation relate the velocity of an enzyme reaction (V) to the concentration of the substrate [S]?
The Michaelis-Menten equation calculates the maximum reaction velocity (Vmax) that can be achieved at a given substrate concentration.
What is the main difference between reversible and irreversible enzyme inhibition?
Reversible inhibition stops when the inhibitor is removed, while irreversible inhibition permanently inactivates the enzyme.
Which of the following statements about competitive inhibitors is correct?
They bind to the active site, preventing the substrate from binding.
Which of the following factors can lead to the denaturation of an enzyme?
Increase in pH beyond the optimum range
What is the effect of increasing the concentration of non-competitive inhibitors on the rate of an enzyme-catalyzed reaction?
The rate decreases as the shape of the enzyme is altered, but not the active site.
What happens to the rate of an enzyme-catalyzed reaction at very high temperatures?
The rate decreases as bonds in the enzyme's tertiary structure break, changing the active site shape.
Which of the following statements about the effect of pH on enzyme activity is correct?
Each enzyme has an optimum pH range, and the rate decreases as the pH moves away from this range.
How do competitive inhibitors affect the rate of an enzyme-catalyzed reaction?
They decrease the rate by binding reversibly to the active site, preventing substrate binding.
Which of the following statements about competitive inhibition is correct?
The inhibitor binds to the active site, preventing the substrate from binding.
How can the effects of competitive inhibition be overcome?
By increasing the concentration of the substrate.
Which of the following is a characteristic of non-competitive inhibition?
The inhibitor binds to a site other than the active site, causing a conformational change.
If an enzyme is inhibited by both a competitive and a non-competitive inhibitor, what would be the effect on the enzyme's $V_{max}$ (maximum velocity)?
$V_{max}$ would decrease, and $K_m$ would increase.
Which of the following statements about enzyme inhibitors is correct?
Inhibitors can be used to control the progress of a reaction.
In a competitive inhibition scenario, what would be the effect of increasing the substrate concentration on the reaction rate?
The reaction rate would increase, and the maximum rate would remain the same.
Test your knowledge on different types of enzyme inhibition, including non-competitive inhibition, feedback inhibition, and reversible inhibition. Learn how inhibitors affect enzyme activity and substrate binding.
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