General Science • BiologyHard
What is the primary mechanism of action of competitive inhibitors on enzyme-catalyzed biochemical reactions?
A. They bind covalently to sites other than the active site, permanently destroying the enzyme tertiary structure
B. They resemble the substrate structurally and reversibly bind to the active site, preventing substrate binding✓ Correct Answer
C. They consume all available cofactor ions required for catalytic activation
D. They alter the optimum temperature of the enzymatic reaction permanently
💡 Solution & Explanation
Competitive inhibitors possess a structural shape and chemical configuration similar to the natural substrate, enabling them to bind reversibly to the active site of the enzyme and block access to the substrate. This inhibition can be overcome by increasing the concentration of the substrate. Non-competitive inhibitors bind to allosteric sites and alter enzyme conformation without competing directly for the active site. Michaelis-Menten kinetics describe how competitive inhibitors increase the apparent KM value without changing Vmax.
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