18 Questions
Which of the following is NOT a characteristic of allosteric regulation of enzymes?
Leads to a linear relationship between substrate concentration and enzyme activity
In the case of uncompetitive inhibition of an enzyme, the inhibitor:
Binds to the enzyme-substrate complex, decreasing the Vmax
Which type of enzyme inhibition results in a decrease in the Km of the enzyme?
Competitive inhibition
Which of the following is a characteristic of noncompetitive inhibition of an enzyme?
The inhibitor binds to the enzyme, decreasing the Vmax
What is the purpose of allosteric regulation in enzymes?
To allow for feedback regulation of the enzyme
Which of the following is a consequence of positive allosteric regulation of an enzyme?
Sigmoidal kinetics
What is the primary factor that regulates the activity of the enzyme phosphofructokinase (PFK) in the glycolysis pathway?
The levels of ADP and AMP in the cell
How does the binding of ATP to phosphofructokinase (PFK) affect the enzyme's activity?
ATP binds to PFK in an allosteric manner, decreasing its activity
Which of the following statements about the effects of citrate on phosphofructokinase (PFK) activity is correct?
Citrate binds to PFK in an allosteric manner, decreasing its activity
Which type of enzyme inhibition is exhibited by the binding of ADP and AMP to phosphofructokinase (PFK)?
Allosteric inhibition
How does the binding of citrate to phosphofructokinase (PFK) affect the enzyme's activity?
Citrate binds to PFK in an allosteric manner, decreasing its activity
Which of the following statements about the regulation of phosphofructokinase (PFK) activity is correct?
PFK is inhibited by high levels of ADP and AMP, indicating the cell has sufficient energy
Which of the following statements about competitive inhibitors is correct?
Competitive inhibitors increase the Michaelis constant (Km) of the enzyme reaction.
What is the effect of a non-competitive inhibitor on an enzyme reaction?
It decreases the maximum velocity (Vmax) but does not affect the Michaelis constant (Km).
Which of the following statements about uncompetitive inhibitors is true?
Uncompetitive inhibitors bind to the enzyme-substrate complex, preventing product formation.
Which of the following factors can affect enzyme activity?
All of the above
What is the difference between allosteric regulation and inhibition in enzymes?
Allosteric regulation involves binding of a molecule to a regulatory site, causing a conformational change, while inhibition involves direct blocking of the active site.
What is the relationship between the Michaelis constant (Km) and substrate affinity?
As Km increases, substrate affinity decreases.
Test your knowledge on the concepts of allosteric regulation involving complex enzymes with regulatory and catalytic subunits, cooperativity, and feedback regulation, along with respiration basics such as catabolism, oxidation, reduction, and electron carriers like NAD+ and FAD.
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