Competitive Inhibition in Enzyme Kinetics

Steps:

• Recall competitive inhibitors bind reversibly to the enzyme's active site, competing with substrate.
• Determine Vmax is unaffected, as high substrate concentrations overcome inhibition.
• Note Km increases due to reduced enzyme-substrate affinity.
• Match to flow diagram: reversible yes leads to Vmax unaffected, selecting B.

Why B is correct:

• Competitive inhibition is reversible and does not alter Vmax, per Michaelis-Menten equation where Vmax = k_cat [E_total], unchanged by inhibitor competition.

Why the others are wrong:

• A: Competitive inhibition does not affect Vmax; it remains constant.
• C: Competitive inhibition is reversible, not irreversible.
• D: Competitive inhibition is reversible and increases Km.

Final answer: B