Reversible inhibitors are molecules that bind to enzymes or receptors temporarily, allowing for the regulation of biological processes. Unlike irreversible inhibitors, which permanently deactivate their targets, reversible inhibitors can detach from the active site, restoring the enzyme's or receptor's function. This property makes them useful in drug design, as they can modulate activity without causing permanent changes. These inhibitors can be classified into competitive, non-competitive, and uncompetitive types, depending on how they interact with the target. For example, competitive inhibitors compete with the substrate for the active site, while non-competitive inhibitors bind to a different site, affecting the enzyme's activity regardless of substrate presence.