Which type of enzyme inhibitors alter the enzyme's shape by binding elsewhere?

Non-competitive inhibitors are a type of enzyme inhibitor that bind to an enzyme at a site distinct from the active site. This binding changes the enzyme's structure, which can reduce its activity, regardless of whether the substrate is bound to the active site. Because non-competitive inhibition does not involve competition with the substrate for the active site, it can inhibit enzymatic activity even when the substrate is present. This is critical in understanding enzyme functionality and regulation, as it shows that the overall activity of an enzyme can be influenced by factors beyond direct substrate interaction.

This contrasts with competitive inhibition, where an inhibitor competes with the substrate for binding to the active site, and reversible and irreversible inhibitors, which refer to the nature and duration of the inhibition rather than the mechanism of how the enzyme's shape is altered. Non-competitive inhibition is particularly important in metabolic pathways, where it allows for finer regulation of enzyme activity in response to varying cellular conditions.