\(\text{K}_{m}\) or Michaelis-Menten constant is the substrate concentration to produce half of the maximum velocity in an enzyme catalyzed reaction.
It shows that half of the enzyme molecules are bound with substrate molecules when substrate concentration equals \(\text{K}_{m}\) value.
A high \(\text{K}_{m}\) value indicates a strong affinity between enzyme and substrate.
The maximum rate of an enzyme reaction is directly proportional to the concentration of enzymes.
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The Correct Option isC
Solution and Explanation
Step 1: Understanding the Concept
The graph shows reaction velocity against substrate concentration. It rises and levels off at \(V_{max}\), and \(K_m\) is the substrate concentration at \(\dfrac{V_{max}}{2}\).
Step 2: Check statements A and B
\(K_m\) is defined as the substrate concentration giving half the maximum velocity, so (A) is correct. At this point half the enzyme molecules are in the ES complex, so (B) is correct.
Step 3: Check statement D
\(V_{max}\) is reached when all enzyme is saturated, so it is directly proportional to the enzyme concentration. (D) is correct.
Step 4: Statement C
A high \(K_m\) means a large substrate concentration is needed for half-maximum velocity, so the enzyme binds the substrate weakly. High \(K_m\) shows low affinity, so (C) is incorrect.
Final Answer:
The incorrect statement is that a high Km indicates strong affinity.
\[ \boxed{\text{(C) }\text{A high K}_{m}\text{ value indicates a strong affinity between enzyme and substrate.}} \]
