Non-competitive inhibition affects enzyme activity by:
Show answer and explanation
Correct answer: Altering enzyme conformation
Non-competitive inhibitors bind to an allosteric site separate from the active site, inducing a conformational change that reduces catalytic efficiency. Because substrate binding is unaffected, Km remains unchanged while Vmax decreases.
Practice all 20 Enzymes: Classification, Kinetics and Inhibition questions
Keep practicing
More Enzymes: Classification, Kinetics and Inhibition questions
- In non-competitive inhibition, Km remains:
- Which inhibition cannot be reversed by increasing substrate concentration?
- Irreversible inhibitors usually bind to enzymes through:
- Which enzyme class catalyzes the breaking of bonds using water?
- Allosteric enzymes differ from Michaelis-Menten enzymes because they:
- The induced-fit model suggests that: