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

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

Research output: Contribution to journalArticle

3 Scopus citations

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 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.

Original languageEnglish (US)
Pages (from-to)537-540
Number of pages4
JournalBioMetals
Volume18
Issue number5
DOIs
StatePublished - Oct 1 2005

Keywords

  • Activation
  • Aryl sulfatase
  • Enzyme activation
  • Helix pomatia
  • Metal ions

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