According to the Michaelis–Menten framework, which inhibition patterns are categorized based on how inhibitors affect Km and Vmax?

Introduction:
Basic enzyme kinetics classifies inhibition by its effect on Km and Vmax. Recognizing standard categories helps diagnose mechanisms from plots or parameter shifts.

Given Data / Assumptions:

• Michaelis–Menten initial-rate conditions.
• Single-substrate model for simplicity.
• Inhibitor binding alters apparent kinetic parameters.

Concept / Approach:
Competitive inhibition increases Km while leaving Vmax unchanged. Pure noncompetitive inhibition decreases Vmax with Km unchanged (mixed forms alter both). Uncompetitive inhibition decreases both Km and Vmax in parallel, often keeping Km/Vmax (slope in some linear plots) constant.

Step-by-Step Solution:
Identify competitive: Km up, Vmax same.Identify noncompetitive (pure): Vmax down, Km same.Identify uncompetitive: Km down, Vmax down in parallel.Conclude that all three are canonical inhibition patterns.

Verification / Alternative check:
Lineweaver–Burk diagnostics: competitive lines intersect at y-axis; noncompetitive lines intersect on x-axis; uncompetitive lines are parallel (for idealized pure forms).

Why Other Options Are Wrong:
Each single option omits other valid patterns; the complete set is “all of the above.”

Common Pitfalls:

• Confusing mixed noncompetitive with pure noncompetitive.
• Forgetting that uncompetitive requires ES binding of inhibitor.

Final Answer:
All of the above