How does a competitive enzyme inhibitor affect the kinetic parameters Km and Vmax in a Lineweaver-Burk plot?
Answer and explanation
Correct answer: B. Increases apparent Km while leaving Vmax unchanged
A competitive inhibitor binds reversibly to the active site, competing with substrate. High substrate concentrations outcompete the inhibitor, so Vmax is unaffected. However, more substrate is required to reach half-maximal velocity, increasing apparent Km.
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