My Biochemistry book mentions that 'competitive inhibition' is a reversible form of inhibition.
But given that the inhibitor is blocking the active site and prevents an enzyme-substrate complex to be formed, how can it be reversible?
A competitive inhibitor typically competes for the active site with the substrate. In this textbook case, binding of a competitive inhibitor is reversible, because it binds to the active site of the enzyme, but is also released, making way for the substrate to bind. The affinity of the substrate, as well as its concentration determine the amount of inhibition (Berg et al., 2002).