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What effect does a competitive inhibitor have on the maximum velocity (vmax) of an enzyme-catalyzed reaction?
What effect does a competitive inhibitor have on the maximum velocity (vmax) of an enzyme-catalyzed reaction?
- It does not alter vmax. (correct)
- It decreases vmax.
- It doubles the vmax.
- It increases vmax.
How can a competitive inhibition be overcome in an enzyme-catalyzed reaction?
How can a competitive inhibition be overcome in an enzyme-catalyzed reaction?
- By removing some inhibitor.
- By lowering the temperature.
- By adding more substrate. (correct)
- By increasing the enzyme concentration.
What happens to the value of Km in the presence of a competitive inhibitor?
What happens to the value of Km in the presence of a competitive inhibitor?
- Km becomes zero.
- Km increases. (correct)
- Km decreases.
- Km remains unchanged.
What is the primary effect of a competitive inhibitor on substrate access to an enzyme?
What is the primary effect of a competitive inhibitor on substrate access to an enzyme?
What is a key characteristic of competitive inhibition regarding affinity?
What is a key characteristic of competitive inhibition regarding affinity?
In a Lineweaver–Burk plot, how does the presence of a competitive inhibitor affect the slope of the line?
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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