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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