Which statement is correct for a non-competitive inhibitor?

The inhibitor binds to the active site of the enzyme and decreases \(\mathrm{V}_{\text {max }}\).

The inhibitor binds away from the active site and increases the Michaelis-Menten constant.

The inhibitor decreases \(\mathrm{V}_{\text {max }}\), but the Michaelis-Menten constant does not change.

The inhibitor does not change \(\mathrm{V}_{\text {max }}\) but increases the Michaelis-Menten constant.

Biology

IGCSE&ALevel

CAIE

Exam No：9700_w24_qp_11 Year：2024 Question No：13

Answer:

Knowledge points:

3.2.1.1 temperature

3.2.1.2 pH (using buffer solutions)

3.2.1.3 enzyme concentration

3.2.1.4 substrate concentration

3.2.1.5 inhibitor concentration

3.2.2 explain that the maximum rate of reaction (Vmax) is used to derive the Michaelis-Menten constant (Km) which is used to compare the affinity of different enzymes for their substrates

3.2.3 explain the effects of inhibitors, both competitive and non- competitive, on the rate of enzyme activity

3.2.4 investigate the difference in activity between an enzyme immobilised in alginate and the same enzyme free in solution, and state the advantages of using immobilised enzymes

Which statement is correct for a non-competitive inhibitor?

Answer:

Knowledge points:

Solution:

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