Select the option that is not correct with respect to enzyme action:
Correct answer: B. The addition of a lot of succinates does not reverse the inhibition of succinic dehydrogenase by malonate
- A. The substrate binds with the enzyme at its active site
- B. The addition of a lot of succinates does not reverse the inhibition of succinic dehydrogenase by malonate
- C. A non-competitive inhibitor binds the enzyme at a site distinct from that which binds the substrate
- D. Malonate is a competitive inhibitor of succinic dehydrogenase
Explanation
The reduction of the activity of succinate dehydrogenase by malonate is an example of competitive inhibition. Competitive inhibition is a reversible inhibition where the inhibitor competes with the normal substrate for the active site of the enzyme. A competitive inhibitor is usually similar to the normal substrate and, therefore, fits into the active site of an enzyme and binds with it. The enzyme can no longer act upon the substrate, and reaction products are not formed. Hence, the action of an enzyme may be reduced or inhibited. Since a competitive inhibitor occupies the site only temporarily, the enzyme action is not permanently affected. Thus, the addition of a lot of succinates can reverse the inhibition of succinic dehydrogenase by malonate.
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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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