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Enzymes and Regulation of Protein Function Quiz
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Which statement best describes the meaning of a low Km value for an enzyme when plotting reaction velocity against substrate concentration?
- A The enzyme has a low affinity for its substrate and requires a high substrate concentration to become saturated You picked ✕
- B The enzyme displays non-Michaelis-Menten kinetics You picked ✕
- C The enzyme reaches half-maximal velocity at a low substrate concentration, indicating high substrate affinity You picked ✓
- D The enzyme only functions effectively at very high substrate concentrations You picked ✕
- E The enzyme has a reduced maximal reaction rate regardless of substrate concentration You picked ✕
Correct!
Incorrect
The answer is C: The enzyme reaches half-maximal velocity at a low substrate concentration, indicating high substrate affinity
Explanation
Why C is correct
See Graphs of enzyme kinetics. Option C is correct. If you plot the velocity (rate) of an enzyme-catalysed reaction against the substrate concentration, the curve rises and then levels off at a ceiling called the maximal velocity, or Vmax, reached when every active site is occupied (saturated). Km is the substrate concentration that gives half of Vmax. A low Km therefore means that only a small amount of substrate is needed to get the enzyme working at half its top speed, which is usually read as a sign of high affinity, meaning the enzyme grips its substrate tightly. A high Km means the reverse: the enzyme needs plenty of substrate before it reaches half its maximum, so its affinity is lower. Km is only an indicator of affinity, not a direct measure of it; it also reflects other aspects of the reaction kinetics, meaning the speeds of the individual steps. The characteristic curve for enzymes that obey the Michaelis-Menten model is a rectangular hyperbola, a curve that climbs steeply and then flattens.
- Meaning of Km: Km is the substrate concentration that gives half of Vmax.
- Low Km: only a little substrate is needed to reach half of top speed, which is usually read as high affinity.
- High Km: more substrate is needed, so the affinity is lower.
- Limit: Km is an indicator of affinity, not a direct measure of it.
Why the other options are incorrect
- A. The enzyme has a low affinity for its substrate and requires a high substrate concentration to become saturated: This describes a high Km, not a low one. An enzyme with low affinity needs a lot of substrate before it is working at half speed. It would be the answer to a question about a high Km. Your answer
- B. The enzyme displays non-Michaelis-Menten kinetics: Km is itself defined from the Michaelis-Menten model, so a Km value does not suggest the enzyme departs from that model. Some enzymes do not obey the model, but a low Km does not signal that. Your answer
- D. The enzyme only functions effectively at very high substrate concentrations: An enzyme that works only at very high substrate concentration has a high Km, because it takes a lot of substrate to reach half of its maximum. A low Km means the opposite: it works well even when substrate is scarce. Your answer
- E. The enzyme has a reduced maximal reaction rate regardless of substrate concentration: Km and Vmax are separate properties. Vmax is the ceiling rate when every active site is occupied, and it depends on the amount of enzyme, so a low Km tells you nothing about a reduced maximum. Your answer
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More questions from this set. Start the quiz to answer them and see each explanation.
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1
For a simple Michaelis–Menten enzyme at fixed enzyme concentration, how does initial rate change as substrate concentration rises?
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2
Which statement best describes the induced fit model of enzyme action?
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