A non-competitive inhibitor binds to an enzyme. What is the expected effect on $V_{max}$ and $K_m$?

💡 Explanation:

Non-competitive inhibitors bind to the enzyme at an allosteric site, not the active site. This alters the enzyme's conformation, reducing its catalytic efficiency (lowering $V_{max}$), but it does not interfere with the substrate's ability to bind to the active site. Therefore, the substrate affinity ($K_m$) remains unchanged. The competitive inhibitor rule is A, and the uncompetitive inhibitor rule is B.