Basically, all reversible inhibitors, competitive and non competitive can regain the enzyme's functionality.
When a reversible inhibitor binds to a enzyme, it is bonded by very weak forces (Van Der Waals forces, basically weak electrostatic forces between molecules, but that's chem I wont get into that). Because these forces are very weak, they tend to disconnect after they bind to the enzyme. When it disconnects it changes the protein back to its original shape and the enzyme gains its functionality.
However, irreversible inhibitors, both non competitive and competitive, permanently inhibit the enzyme when they bind because they form covalent bonds. Unlike the weak forces that hold reversible inhibitors to enzyme, these covalent bonds do not disconnect from the enzyme because its a strong bond. Therefore the shape is changed permanently and it won't regain its functionality.
Idk if I explained that well. if something that I said doesn't make sense, please ask
