Expression of human estrogen sulfotransferase in Salmonella typhimurium: differences between hHST and hEST in the enantioselective activation of 1-hydroxyethylpyrene to a mutagen

Chem Biol Interact. 1998 Feb 20;109(1-3):249-53. doi: 10.1016/s0009-2797(97)00136-1.

Abstract

Various human sulfotransferases (hP-PST, hM-PST, hHST) and rat sulfotransferases (rPST-IV, rHSTa) have already been expressed in Ames' Salmonella strains (in particular in TA1538). Now a further strain, TA1538-hEST, which expresses the human estrogen sulfotransferase (hEST), has been constructed. This strain activated the primary benzylic alcohol 1-hydroxymethylpyrene (1-HMP) and the secondary benzylic alcohol 1-hydroxyethylpyrene (1-HEP) to mutagens. Human sulfotransferases hEST and hHST both activated 1-HEP, but they differed substantially in their enantioselectivity for this compound.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Benzyl Alcohols / pharmacokinetics
  • Benzyl Alcohols / toxicity
  • Blotting, Western
  • Cytosol / enzymology
  • Humans
  • Mutagenicity Tests
  • Mutagens / pharmacokinetics*
  • Mutagens / toxicity
  • Rats
  • Salmonella typhimurium / drug effects
  • Salmonella typhimurium / enzymology*
  • Salmonella typhimurium / genetics
  • Stereoisomerism
  • Substrate Specificity
  • Sulfotransferases / biosynthesis
  • Sulfotransferases / genetics
  • Sulfotransferases / metabolism*

Substances

  • Benzyl Alcohols
  • Mutagens
  • Sulfotransferases
  • alcohol sulfotransferase
  • estrone sulfotransferase