Question 1

Q: Which of the following is true about non-competitive inhibition?

Km remains same, Vmax decreases. ***Km remains same, Vmax decreases*** - In **non-competitive inhibition**, the inhibitor binds to an allosteric site on the enzyme, altering its conformation, thereby **reducing its catalytic efficiency**. - This binding does not affect the **enzyme's affinity for the substrate (Km remains the same)**, but it **reduces the maximum reaction rate (Vmax decreases)** because fewer enzyme molecules are able to perform catalysis per unit time. *Km increases, Vmax remains same* - This describes **competitive inhibition**, where the inhibitor competes with the substrate for the enzyme's active site. - While it **increases the apparent Km** (more substrate needed to reach half Vmax), **Vmax remains unchanged** as high substrate concentrations can overcome the inhibition. *Km decreases, Vmax increases* - This scenario would imply an activation rather than inhibition, where both enzyme affinity and catalytic efficiency are enhanced. - This is not characteristic of any standard **enzyme inhibition mechanism**. *Km increases, Vmax increases* - This combination is not observed in any typical **enzyme inhibition pattern**. - An increase in **Vmax** implies enhanced catalytic activity, while an increase in **Km** suggests reduced substrate affinity, which are contradictory effects for a single inhibitor.

Question

Which of the following is true about non-competitive inhibition?

Accepted Answer

Km remains same, Vmax decreases

Answer

Km increases, Vmax remains same

Answer

Km decreases, Vmax increases

Answer

Km increases, Vmax increases

INI-CET 2024 — Biochemistry