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What is competitive inhibition in the context of enzyme activity?
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Competitive inhibition occurs when a substance mimics the substrate of an enzyme, competing for binding at the active site and reducing the enzyme's activity.
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How does competitive inhibition affect the Km of an enzyme-catalyzed reaction?
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Competitive inhibition increases the apparent Km of the enzyme without affecting Vmax.
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Can Vmax be achieved in the presence of a competitive inhibitor?
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Yes, Vmax can still be achieved in competitive inhibition by increasing substrate concentration.
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How does competitive inhibition differ from non-competitive inhibition?
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In competitive inhibition, the inhibitor binds the active site, whereas, in non-competitive inhibition, the inhibitor binds elsewhere on the enzyme.
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What is an example of a competitive inhibitor in pharmacology?
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Methotrexate is a competitive inhibitor of dihydrofolate reductase, an enzyme involved in nucleotide synthesis.
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How do enzymes overcome competitive inhibition in nature?
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Enzymes can overcome competitive inhibition by increasing the concentration of the natural substrate.
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How does competitive inhibition appear on a Lineweaver-Burk plot?
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In competitive inhibition, Lineweaver-Burk plots show lines with the same y-intercept but different slopes (increased Km).
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Is competitive inhibition reversible?
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Yes, competitive inhibition is typically reversible.
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What does a low Ki value indicate about a competitive inhibitor?
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A low Ki value indicates a strong inhibitor, requiring lower concentrations to effectively inhibit enzyme activity.
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What structural characteristics make a molecule a good competitive inhibitor?
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Structural similarity to the enzyme's substrate makes a molecule a good competitive inhibitor.
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In the context of enzyme inhibition, what is allosteric inhibition, and how does it differ from competitive inhibition?
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Allosteric inhibition involves inhibitors binding to a site other than the active site, different from competitive inhibition where the inhibitor binds the active site.
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What role does competitive inhibition play in regulating metabolic pathways?
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Competitive inhibition plays a role by controlling the flux through pathways based on substrate and inhibitor availability.
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How does competitive inhibition relate to enzyme specificity?
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Competitive inhibition highlights the importance of enzyme specificity since inhibitors must closely resemble the substrate to compete effectively.
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What is the biological significance of competitive inhibition?
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Competitive inhibition regulates enzyme activity and thus plays a crucial role in controlling metabolic processes.
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Can a competitive inhibitor be used as a drug to modulate enzyme activity?
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Yes, competitive inhibitors are often used as drugs to selectively reduce enzyme activity in various conditions.
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