What type of inhibitors compete with the natural substrate for enzyme binding?

Competitive inhibitors bind to the active site of an enzyme, competing directly with the natural substrate for that site. This interaction prevents the substrate from attaching, thereby inhibiting the enzyme's activity. The degree of inhibition depends on the relative concentrations of the inhibitor and the substrate. If the concentration of the substrate is increased, it can outcompete the inhibitor for binding to the enzyme, leading to a decrease in the effects of the inhibition.

This competition is a defining characteristic of competitive inhibition, which contrasts with other types of inhibition. For instance, non-competitive inhibitors bind to a different part of the enzyme, not at the active site, and do not directly compete with the substrate. Allosteric inhibitors also bind to sites other than the active site and can change the enzyme's shape or activity, but they do not compete for binding. Reversible inhibitors can include competitive and non-competitive types, but in this context, identifying the specific behavior related to substrate competition clearly points to competitive inhibitors.