Which of the following statements about Competitive and noncompetitive inhibition is false? a. A noncompetitive inhibitor does not change the Km of the enzyme. b. A competitive inhibitor does not change the Vmax of the enzyme c. The noncompetitive inhibitor can bind either free enzyme or the enzyme–substrate complex. d.A competitive inhibitor decreases the apparent Km for a given substrate.

When measuring reaction velocity as a function of substrate concentration, a researcher usually keeps the concentration of enzyme at a constant level. What would happen if the enzyme concentration were not kept constant? A. Vmax would change, but Km would remain constant. B. Both Vmax and Km would change C. Vmax would remain constant, but Km would change D. Vmax would remain constant, but V would change E. None of the above would necessarily occur

What is true about a competitive inhibitor of an enzyme? You can choose more than one a. it binds the active site b. it binds an allosteric site c. it physically blocks the substrate d. it warps the active site e. it can be overcome with large amounts of substrate

In drug development, enzyme inhibition studies play a very important role since drugs are often used to target specific enzymes, as illustrated in the example of lovastatin. An important consideration when assessing drug potential is the drug's affinity for the selected target. (The higher the affinity, the better the candidate.) The K₁ is often used in studies to measure the affinity of drug candidates toward their target. Based on your understanding of K₁, which drug would be the BEST candidate for further development? Drug C: K₁= 9.1 x 107 M Drug E: K₁ = 3.5 × 10³ mm Drug D: K₁=5.5 × 10³ μM Drug B: K₁=2.5 × 10 mm Drug A: K₁=4.5 x 10 mm