Evidence for the Cd(2+) 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. E...

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Bibliographic Details
Published in:Biometals 2005-10, Vol.18 (5), p.537-540
Main Authors: Tokheim, Abigail M, Spannaus-Martin, Donna J, Martin, Bruce L
Format: Article
Language:English
Subjects:
Animals
Arylsulfatases - chemistry
Arylsulfatases - drug effects
Arylsulfatases - metabolism
Cadmium - chemistry
Cadmium - metabolism
Cadmium - pharmacology
Catalysis
Chymotrypsin - antagonists & inhibitors
Copper - chemistry
Copper - metabolism
Copper - pharmacology
Dose-Response Relationship, Drug
Enzyme Activation - drug effects
Esterases - antagonists & inhibitors
Galactosidases - antagonists & inhibitors
Helix (Snails) - enzymology
Zinc - chemistry
Zinc - metabolism
Zinc - pharmacology
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Summary: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.
ISSN:0966-0844
DOI:10.1007/s10534-005-0836-0