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Questions and Answers
What does a higher value of $K_m$ indicate about an enzyme's affinity for its substrate?
What does a higher value of $K_m$ indicate about an enzyme's affinity for its substrate?
- It shows that the enzyme has a higher turnover number.
- It suggests the enzyme is less effective with substrate.
- It indicates a lower affinity for the substrate. (correct)
- It indicates a higher catalytic efficiency.
How does competitive inhibition specifically affect the Michaelis-Menten kinetics?
How does competitive inhibition specifically affect the Michaelis-Menten kinetics?
- $K_m$ increases while $V_{max}$ remains unchanged. (correct)
- $K_m$ remains unchanged and $V_{max}$ decreases.
- $K_m$ increases and $V_{max}$ increases.
- $K_m$ decreases and $V_{max}$ decreases.
What is the steady state assumption in enzyme kinetics?
What is the steady state assumption in enzyme kinetics?
- The enzyme's activity decreases as substrate concentration decreases.
- The concentration of the substrate remains constant over time.
- The formation of products is greater than substrate consumption.
- The rate of formation of the enzyme-substrate complex is equal to the rate of its breakdown. (correct)
What is the fundamental difference between $k_{cat}$ and catalytic efficiency?
What is the fundamental difference between $k_{cat}$ and catalytic efficiency?
Which statement correctly describes the effect of uncompetitive inhibition on enzyme kinetics?
Which statement correctly describes the effect of uncompetitive inhibition on enzyme kinetics?
Flashcards
Michaelis-Menten Equation
Michaelis-Menten Equation
Describes how the rate of an enzyme-catalyzed reaction depends on substrate concentration.
Steady State Assumption
Steady State Assumption
Enzyme-substrate complex formation and breakdown occur at equal rates.
Km
Km
Substrate concentration at which the reaction rate is half of Vmax.
kcat
kcat
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Competitive Inhibitor
Competitive Inhibitor
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Study Notes
Enzyme Kinetics
- Understand enzyme saturation curves
- Discuss assumptions of enzyme kinetics
- Understand the Michaelis-Menten equation (no derivation needed)
- Define steady-state assumption
- Define Km and explain its meaning
- Explain what Km tells about the enzyme and the substrate
- Define kcat
- Define catalytic efficiency
- Define turnover number
- Calculate Km and Vmax from a Lineweaver-Burke plot, including units
- Explain how a competitive inhibitor affects Vmax and Km
- Explain how a uncompetitive inhibitor affects Vmax and Km
- Explain how a non-competitive inhibitor affects Vmax and Km
- Recognize Lineweaver-Burke plots for each inhibition type
- Discuss enzyme regulations
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