medium · MCAT bio-biochem
An enzyme-catalyzed reaction follows Michaelis-Menten kinetics.
If a researcher adds a reversible inhibitor that increases the apparent K_M but leaves the V_max unchanged, which of the following describes the interaction between the inhibitor and the enzyme?
- The inhibitor binds to an allosteric site regardless of whether the substrate is present.
- The inhibitor binds to the active site and prevents substrate binding.
- The inhibitor covalently binds to the enzyme, permanently deactivating it.
- The inhibitor binds to an allosteric site only after the substrate has bound.
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