In non-competitive enzyme inhibition, how are the parameters and affected by the presence of a reversible non-competitive inhibitor?
Answer and explanation
Correct answer: A. decreases while remains unchanged
- Step 1: A non-competitive inhibitor binds to an allosteric site located away from the catalytic active site.
- Step 2: It binds with equal affinity to both the free enzyme () and the enzyme-substrate complex (), meaning it does not interfere with substrate binding ( unchanged).
- Step 3: Because the resulting complex is catalytically inactive, the effective concentration of functioning enzyme is reduced, causing to decrease.
Answer
decreases while remains unchanged.
Why not the others: unchanged while increases describes competitive inhibition; Both increasing is physiologically impossible for an inhibitor; Both decreasing describes uncompetitive inhibition.
Practise more Biomolecules and Enzymes.
Free questions with an explanation for every one, and full timed NEET UG mock tests.
More Biomolecules and Enzymes questions
- In competitive enzyme inhibition, how do the Michaelis constant () and the maximum velocity () change in the presence of the i…
- Which classic example illustrates competitive inhibition of an enzyme by a substrate analog?
- According to the B-DNA structural model described by Watson and Crick, what are the pitch of the helix and the distance between two successi…
- Which of the following nitrogenous bases is a double-ring purine derivative found in both DNA and RNA?
- Why does cellulose fail to give a blue color with iodine solution, whereas starch produces an intense blue complex?
- Lecithin, an essential component of the alveolar surfactant and cellular membranes, is classified chemically as a: