Questions and Answers
What effect does a competitive inhibitor have on the maximum velocity (vmax) of an enzyme-catalyzed reaction?
How can a competitive inhibition be overcome in an enzyme-catalyzed reaction?
What happens to the value of Km in the presence of a competitive inhibitor?
What is the primary effect of a competitive inhibitor on substrate access to an enzyme?
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What is a key characteristic of competitive inhibition regarding affinity?
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In a Lineweaver–Burk plot, how does the presence of a competitive inhibitor affect the slope of the line?
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Study Notes
Competitive Inhibition
- Competitive inhibition occurs when an inhibitor occupies the active site of an enzyme, preventing substrate binding.
- The presence of an inhibitor blocks substrate access to the enzymatic binding site, hindering the reaction.
- Increasing substrate concentration can outcompete the inhibitor; higher substrate-to-inhibitor ratios enhance the likelihood of substrate binding.
- If the enzyme has equal affinity for both substrate and inhibitor, more substrate increases chances of enzyme-substrate complex formation.
- The maximum reaction velocity (Vmax) remains unchanged despite the presence of a competitive inhibitor, as sufficient substrate can always outcompete the inhibitor.
- Inhibitor presence raises the Michaelis constant (Km), indicating that a higher substrate concentration is required to achieve half of Vmax during inhibition.
- A Lineweaver–Burk plot illustrates the effect of competitive inhibition by showing altered Km values while Vmax stays constant.
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Description
This quiz explores the concept of competitive inhibition in enzyme activity. Learn how inhibitors affect substrate binding and how varying substrate concentrations can influence enzymatic reactions. Test your knowledge on the dynamics of enzyme inhibition.
