Enzymes are biological catalysts, meaning they speed up chemical reactions that are necessary for life. Without enzymes, these reactions would happen too slowly to sustain living organisms.
One way our bodies regulate these reactions is through enzyme inhibition. This is a process where molecules called inhibitors bind to enzymes, reducing their activity and slowing down the rate of the reaction.
There are two main types of enzyme inhibitors: reversible and irreversible. Reversible inhibitors bind to enzymes non-covalently, meaning their binding is temporary. Irreversible inhibitors, on the other hand, bind covalently, forming a strong, permanent bond with the enzyme.
This article will focus on two types of reversible inhibition: noncompetitive vs uncompetitive inhibition. We’ll explore how each type of inhibitor works and how they affect enzyme activity.