In order to construct high activity smart artificial enzyme, schistosoma japonicum glutathione sulfotransferase (sjGST) was selected as the artificial enzyme skeleton and lysine at position of 124 was mutated to cysteine. pH-responsive supramolecular switch based on cucurbit[6] uril was modified exactly to the catalytic pocket of the artificial enzyme skeleton by a click chemistry reaction at pH = 6.0. The large and rigid switch molecule could effectively prevent the substrate from entering the catalytic pocket. Activity of artificial enzyme was "closed" as sjGST show only 3% catalytic activity at this time. The supramolecular switch was dissociated at pH = 7.5 resulting in cucurbit[6] uril to be away from catalytic pocket. The substrate could enter the catalytic pocket freely at this time. Activity of artificial enzyme was "open" as sjGST show more than 90% catalytic activity at this time. The reversible close and open of the artificial enzyme activity could be still achieved after 5 cycles of repeated regulation of the system pH between 6.0 and 7.5. As a result, the reversible close and open regulation of sjGST catalytic activity was successfully achieved utilizing the association and dissociation of supramolecular switch. By this way a high activity pH-responsive smart artificial enzyme was successful constructed.