How does competitive enzyme inhibition affect a chemical reaction?

Competitive inhibitors hinder a chemical reaction by attaching themselves to the active site of an enzyme and restricting the substrate from binding. These inhibitors often mimic the structural features of the enzyme's natural substrate, allowing them to bind strongly to the active site. Essentially, they compete with the substrate for binding to the enzyme's active site by imitating its shape and characteristics. This interference caused by inhibitors can occur in two ways: reversible or irreversible binding.

In reversible inhibition, the inhibitor binds to the enzyme in a way that allows it to detach, restoring the enzyme's activity. It can compete with the substrate for the active site or attach to a different site on the enzyme. The bond formed between the inhibitor and the enzyme is temporary and can be broken, enabling the enzyme to resume its normal function once the inhibitor is released. Irreversible inhibitors form strong, typically covalent bonds with the enzyme, permanently altering its structure or blocking its active site.