medium · MCAT bio-biochem
An enzyme obeys Michaelis-Menten kinetics. A reversible inhibitor is added that, at a fixed concentration, lowers the apparent V_max to one-half but leaves the apparent K_m unchanged. The substrate is then raised to a very high, saturating concentration. Compared with the uninhibited enzyme at the same saturating substrate, the inhibited reaction velocity will be:
- Equal, because saturating substrate fully outcompetes the inhibitor and restores the original rate
- Half, because the inhibitor's effect on V_max cannot be overcome by increasing substrate
- Lower but recoverable toward the original V_max as substrate is raised further beyond saturation
- Indeterminate without knowing K_m, since the velocity depends on the K_m-to-substrate ratio
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