Evidence for the Cd²⁺ activation of the aryl sulfatase from helix pomatia

Often used to remove sulfate groups from carbohydrates, the regulatory properties of the aryl sulfatase from Helix pomatia remain little characterized. As many hydrolytic enzymes utilize exogenous metal ions in catalysis, the effect of various divalent metal ions on the sulfatase was investigated. Evidence for metal ion activation was collected, with Cd²⁺ being notable for effective activation. The enzyme was inhibited by Cu²⁺. The response of other common hydrolases to divalent metal ions was characterized. Activation by Cd²⁺ was not observed for chymotrypsin, rabbit liver esterase, or β-galactosidase. Instead, Cd was found to inhibit both the esterase and the galactosidase. Inhibition by Cu²⁺ and Zn²⁺ was also observed for some of these hydrolases.