Practice Enzyme Kinetics (michaelis–menten Basics) (6.1)

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6 sample questions

Question 1.
What is Vmax in enzyme kinetics?
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Think about what happens when all enzyme active sites are occupied.
Question 2.
Define Km.
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Consider it a measure of the enzyme's affinity for its substrate.
3Question 3.
What does Vmax represent in enzyme kinetics?
- The rate of reaction at half maximum velocity
- The maximum rate of reaction
- The minimum rate of reaction
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Think about the capacity of an enzyme at saturation.
4Question 4.
True or False: Km represents the substrate concentration at which the reaction rate is half of Vmax.
- True
- False
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Consider what happens when you adjust the substrate concentration.
Question 5.
Given a set of data points for reaction rates and substrate concentrations, derive Km and Vmax using the Lineweaver-Burk plot.
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Remember that slope = Km/Vmax and intercept = 1/Vmax.
Question 6.
Explain how a competitive inhibitor alters the kinetic parameters of an enzyme-catalyzed reaction.
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Think about how inhibitors interact at the active site.

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