A Levels Biology (9700)•9700/12/O/N/23

Explanation
Understanding Km in enzyme kinetics Steps:
- Recall Km definition: substrate concentration at half Vmax in Michaelis-Menten equation.
- Evaluate statement 1: Km indicates enzyme-substrate affinity (lower Km means higher affinity)—correct.
- Evaluate statement 2: Km equals enzyme's turnover number—incorrect, as Km relates to binding, not kcat.
- Evaluate statement 3: Km is always the dissociation constant Kd—incorrect, as Km = (k-1 + kcat)/k1, not just Kd.
- Evaluate statement 4: Km remains constant with enzyme concentration changes—correct, as it's intrinsic to the enzyme-substrate interaction.
Why B is correct:
- B selects statements 1 and 4, matching the accurate definitions of Km as affinity measure and concentration-independent parameter.
Why the others are wrong:
- A includes 2 and 3, which confuse Km with turnover and Kd.
- C omits 4 and includes incorrect 3.
- D includes incorrect 2 and omits 1.
Final answer: B
Topic: Mode of action of enzymes
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