To ensure that the body’s systems work correctly, sometimes enzymes need to be slowed down. For instance, if an enzyme is making too much of a product, there needs to be a way to reduce or stop production.
Enzymes’ activity can be inhibited in a number of ways:
Competitive inhibitors – a molecule blocks the active site so that the substrate has to compete with the inhibitor to attach to the enzyme.
Non-competitive inhibitors – a molecule binds to an enzyme somewhere other than the active site and reduces how effectively it works.
Uncompetitive inhibitors – the inhibitor binds to the enzyme and substrate after they have bound to each other. The products leave the active site less easily, and the reaction is slowed down.
Irreversible inhibitors – an irreversible inhibitor binds to an enzyme and permanently inactivates it.