Protons behave as competitive-type inhibitors of tyrosinase.
Tyrosinase pK<sub>asub> causes a sigmoidal behavior in the dependence of initial rate vs. pH.
E322 could be responsible for the pH effect acting as a gatekeeper.
A bell-shaped dependence occurs if the pK<sub>asub> of the phenolic hydroxyl groups are low.
Negatively charged substrates in the R group cooperate in the bell-shaped behavior.