Binuclear metallohydrolases are a structurally diverse group of enzymes that use binuclear metal ion centers to catalyze the hydrolysis of amides and esters of carboxylic and phosphoric acids. Representatives are listed in Table 1, together with their metal ion composition and, if known, their metabolic role (s). Several of these enzymes are either targets for drug design against a wide variety of human disorders, including osteoporosis, cancer, cystic fibrosis, and depression, or are of significance in bioremediation since they can be modified to degrade pesticides or organophosphorus nerve gases.

In 1996, Wilcox summarized the then current knowledge about the structure, function, and mechanism of all known binuclear metallohydrolases. 1 In subsequent years more specialized articles followed, 2 focusing on the binuclear manganese-containing arginases, catalases, and enolases, 3 the Ser/Thr protein phosphatases (in particular calcineurin), 4-6