Which of the following best describes an allosteric enzyme?
Correct answer: C. Its activity is altered by binding of an effector molecule at a site other than the active site
- A. It has only one binding site
- B. It is regulated by covalent modification
- C. Its activity is altered by binding of an effector molecule at a site other than the active site
- D. It follows Michaelis-Menten kinetics strictly
Explanation
Allosteric enzymes have an allosteric site (different from the active site) where regulators (activators or inhibitors) bind, causing a conformational change that modulates activity. They often don't follow simple Michaelis-Menten kinetics.
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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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