hard · 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
Sign up free to see the explanation and track your rank →
More MCAT bio-biochem practice
- What genetic term describes a single gene influencing multiple seemingly unrelated traits?
- In the human ear, sound waves cause fluid in the cochlea to… — Which cells are responsible
- An electrophysiologist observes a neuron at its resting memb… — Which ion is primarily res
- Which structure is most likely dysfunctional?
- Which organelle would you expect to be exceptionally well-developed in these cells?
- Which molecule acts as a 'fluidity buffer' in animal cell membranes?
- A scientist is tracking the movement of a secreted protein. If the protein has just left t
- A molecule moves into a cell against its concentration gradient using energy provided by a