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A competitive inhibitor affects enzyme kinetics by

Answer: Increasing Km only.

  • A Decreasing Vmax only
  • B Increasing Km only
  • C Decreasing both Km and Vmax
  • D Increasing both Km and Vmax

Correct answer: B. Increasing Km only

Explanation: Competitive inhibitors compete with substrate for the active site. They increase apparent Km (lower affinity) but do not affect Vmax (can be overcome by excess substrate).

Enzyme Kinetics: Rate vs Substrate Concentration[Substrate]Reaction rateVmaxKm½VmaxCurve flattens at high [S]: ALL enzyme active sites are occupied (saturation)

As substrate concentration rises, reaction rate increases steeply at first, then plateaus at Vmax once every enzyme molecule is working at full capacity; Km is the substrate concentration giving half-maximal rate, and a LOWER Km means the enzyme reaches that rate with less substrate (higher affinity).

Concept context

Carbohydrates, proteins, lipids, nucleic acids, and enzyme kinetics. Essential foundation for understanding metabolism.

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