Final answer:
The statement that almost all ERIC inhibitors block the active site is false since inhibitors can act in different ways, including competitively at the active site or allosterically at a different site, leading to enzyme inactivation.
Step-by-step explanation:
The statement that almost all ERIC inhibitors block the active site is false. Inhibitors can bind in various ways to enzymes. A competitive inhibitor most closely resembles the substrate and competes for the active site, directly blocking it, which prevents the substrate from binding. On the other hand, an allosteric inhibitor binds to a different site on the enzyme, not the active site. This interaction leads to a change in the enzyme's conformation, reducing its affinity for the substrate and thus indirectly blocking the active site.
It's important to understand that not all inhibitors work by blocking the active site; they can function through different mechanisms such as allosteric inhibition where they bind away from the active site, or covalent modification where they bind irreversibly to the active site. The effect of inhibitor binding is generally to inactivate the enzyme, thereby reducing or preventing the enzyme's ability to catalyze a reaction.