Question: Describe how allosteric regulation differs from competitive inhibition in enzyme kinetics, and provide examples of how these mechanisms affect metabolic pathways

Question

Question is about enzymes

Answer 1

A competitive inhibitor binds to the enzyme's active site, preventing the substrate from

binding. This type of inhibition can be overcome by increasing the concentration of the

substrate.

An allosteric inhibitor binds to a site on the enzyme other than the active site, causing

a conformational change that reduces the enzyme's activity.