In mixed inhibition, the allosteric effect affects the _.
Correct answer: C. Shape of enzyme
- A. Shape of substrate
- B. Shape of inhibitor
- C. Shape of enzyme
- D. None of these
Explanation
In mixed inhibition, the inhibitor binds to an allosteric site, i.e. a site different from the active site where the substrate binds.This causes the denaturation of the enzyme's 3D shape. Hence, option C is correct
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Enzymes are biological catalysts that lower activation energy without being consumed, and their specificity is explained by the lock and key and induced fit models. Work includes the effects of temperature, pH and substrate concentration on reaction rate, plus competitive and non-competitive inhibition and how these differ.
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