MHT CET 202622 AprilMorning Shift
- Exam
- MHT CET
- Year
- 2026
- Date
- 22 April
- Shift
- Morning Shift
- Subject
- Biology
- Chapter
- Biomolecules (B)
MHT CET 2026 · 22 April · Morning Shift · Biology · Biomolecules (B)
Which one of the following statements is INCORRECT based on the...
Which one of the following statements is INCORRECT based on the above graph showing the rate of enzyme action?
Options
- A or Michaelis-Menten constant is the substrate concentration to produce half of the maximum velocity in an enzyme catalyzed reaction.
- BIt shows that half of the enzyme molecules are bound with substrate molecules when substate concentration equals value.
- CA high value indicates a strong affinity between enzyme and substrate.
- DThe maximum rate of an enzyme reaction is directly proportional to the concentration of enzymes.
Correct answer
C. A high value indicates a strong affinity between enzyme and substrate.
Step-by-step solution
The Michaelis-Menten constant (K_m) is defined as the substrate concentration at which the reaction rate is half of its maximum velocity (V_\max/2). This directly supports statement (1).
At , the reaction rate is V_\max/2. This means that exactly half of the active sites on the enzyme molecules are occupied by substrate molecules. This supports statement (2).
The maximum rate of an enzyme-catalyzed reaction (V_\max) is directly proportional to the total concentration of the enzyme present (V_\max = k_{cat} \times [E]_{total}). This supports statement (4).
The value is an inverse measure of the affinity of an enzyme for its substrate. A lower value indicates that a lower concentration of substrate is needed to reach half the maximum velocity, meaning the enzyme has a high affinity for the substrate. Conversely, a high value indicates a weak affinity between the enzyme and the substrate, as more substrate is required to achieve V_\max/2. Therefore, statement (3) is incorrect.
Answer: A high value indicates a strong affinity between enzyme and substrate.
At , the reaction rate is V_\max/2. This means that exactly half of the active sites on the enzyme molecules are occupied by substrate molecules. This supports statement (2).
The maximum rate of an enzyme-catalyzed reaction (V_\max) is directly proportional to the total concentration of the enzyme present (V_\max = k_{cat} \times [E]_{total}). This supports statement (4).
The value is an inverse measure of the affinity of an enzyme for its substrate. A lower value indicates that a lower concentration of substrate is needed to reach half the maximum velocity, meaning the enzyme has a high affinity for the substrate. Conversely, a high value indicates a weak affinity between the enzyme and the substrate, as more substrate is required to achieve V_\max/2. Therefore, statement (3) is incorrect.
Answer: A high value indicates a strong affinity between enzyme and substrate.