Crayfish astacin is a unique small Zn2+ endopeptidase (MW = 22 kDa) found in the digestive fluid of crustaceans, and belongs to the only Zn protein family that contain a coordinated Tyr under physiological conditions [1] (see structure). However, the presence of a negatively charged phenolate, i.e., the coordinated Tyr, is known to decrease the Lewis acidity of the metal ion in metal complexes [2,3]. As a result, a decrease in water activation by ~2 orders in terms of the pKa of the coordinated water has been observed in metal complexes. This decrease in Lewis acidity of the metal by a coordinated phenolate should presumably result in a significant decrease in metal-centered hydrolytic activity. On the contrary, this is not the case in phenolate(Tyr)-coordinated astacin which still exhibits high hydrolytic activity under neutral conditions. Hence, the coordinated Tyr may not act to lower the Lewis acidity of the active-site metal in astacin during its catalysis, but may play some unique roles in the action of astacin that have not yet been observed in other metalloproteases. A better understanding of the roles of this coordinated Tyr is essential to provide further insight into the catalysis of astacin family