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Evidence for the Cd(2+) Activation of the Aryl Sulfatase From Helix Pomatia

Evidence for the Cd(2+) Activation of the Aryl Sulfatase From Helix Pomatia

Abigail M Tokheim, Donna J Spannaus-Martin, Bruce L Martin

Biometals. 2005 Oct;18(5):537-40.

PMID: 16333754

Abstract:

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 Cd(2+) being notable for effective activation. The enzyme was inhibited by Cu(2+). The response of other common hydrolases to divalent metal ions was characterized. Activation by Cd(2+) was not observed for chymotrypsin, rabbit liver esterase, or beta-galactosidase. Instead, Cd was found to inhibit both the esterase and the galactosidase. Inhibition by Cu(2+) and Zn(2+) was also observed for some of these hydrolases.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9016175	Sulfatase from Helix pomatia		9016-17-5	Price

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