This type of inhibition is _______________.

We know because __________________.

In this type of inhibition, ___________ is forbidden.

Question

This type of inhibition is _______________.

We know because __________________.

In this type of inhibition, ___________ is forbidden.

BlackTom AI · Accepted Answer

Competitive inhibition increases the apparent Km without changing Vmax, so the inhibitor and substrate compete for the same active site and the ESI complex cannot form.

1) Relevant knowledge points and concepts
- Michaelis–Menten kinetics: Vmax is the maximal velocity; Km is the substrate concentration at half Vmax and reflects substrate affinity.
- Competitive inhibition: inhibitor binds to the free enzyme (E) at the active site, blocking substrate binding; it does not bind to ES. This raises the apparent Km (lower apparent affinity) but leaves Vmax unchanged.
- Quantitative relation: Km,app = Km × (1 + [I]/Ki) for competitive inhibition; Vmax,app = Vmax.

2) Step-by-step reasoning using the graph
- The black curve (no inhibitor) reaches a certain asymptotic Vmax.
- The red curve (with inhibitor) approaches the same Vmax at very high [S] (same asymptote), indicating Vmax is unchanged.
- At lower/mid [S], the inhibited curve is shifted to the right: more substrate is needed to reach half the maximal velocity, so Km,app is larger.

3) Intermediate calculation/derivation
- From the competitive inhibition formula: Km,app = Km × (1 + [I]/Ki). As [I] > 0, (1 + [I]/Ki) > 1, therefore Km,app > Km.
- Vmax,app = Vmax because at sufficiently high [S] the substrate outcompetes the inhibitor for E.

4) Why the correct answer is correct
- The graph shows an increase in Km (right shift) with unchanged Vmax → hallmark of competitive inhibition. Because inhibitor binds only to E and not ES, formation of the ESI complex is forbidden.

5) Why other options are incorrect
- “Not-competitive” is wrong: noncompetitive inhibition lowers Vmax while leaving Km unchanged (graph would show lower asymptote).
- Options that state “EI” is forbidden are wrong: EI (enzyme–inhibitor) does form in competitive inhibition; what is forbidden is ESI (enzyme–substrate–inhibitor) because inhibitor and substrate cannot bind simultaneously to the same active site.
- Any choice claiming Vmax is lowered contradicts the graph’s unchanged asymptote.

6) Conclusion
- Therefore the correct choice is: competitive, Km-app is larger and Vmax is unchanged, ESI — which matches the provided answer.

This type of inhibition is ___. We know because . In this type of inhibition, _ is forbidden.单项选择题

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This type of inhibition is _______________. We know because __________________. In this type of inhibition, ___________ is forbidden.单项选择题

类似问题

How does a competitive inhibitor affect Km and Vmax ?

Which type of enzyme inhibitor does not affect the maximal velocity of a reaction?

Which of the following sentences best describes what happens during competitive inhibition of an enzyme?

A competitive inhibitor of an enzyme:

A competitive inhibitor of an enzyme:

9. This figure describes inhibition of an enzyme by ____________________.

更多留学生实用工具

希望你的学习变得更简单

This type of inhibition is ___. We know because . In this type of inhibition, _ is forbidden.单项选择题