Compared with the uninhibited enzyme, a non competitive inhibitor
Correct answer: D. lowers Vmax and leaves Km unchanged
- A. raises Vmax and leaves Km unchanged
- B. raises both Vmax and Km
- C. lowers Km and leaves Vmax unchanged
- D. lowers Vmax and leaves Km unchanged
Explanation
Because the inhibitor binds elsewhere and cannot be displaced by substrate, a fraction of the enzyme is permanently out of action, so the maximum achievable rate falls while the affinity of the remaining active sites for the substrate is unaltered. A competitive inhibitor shows the opposite pattern, an unchanged Vmax with an apparently raised Km. This pair of effects is the standard way of telling the two kinds apart in the laboratory.
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About Enzyme Inhibitors
Enzyme inhibitors reduce reaction rate by interfering with enzyme-substrate interaction or catalytic activity. Coverage includes reversible competitive, non-competitive and uncompetitive inhibition, the effects of inhibitor concentration on reaction rate, and why competitive inhibition can be reduced by increasing substrate concentration.
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