Effects of 3'-phosphoadenosine 5'-phosphate on the activity and folding of phenol sulfotransferase

Yuh-Shyong Yang*, Shauo Wei Tsai, En Shyh Lin

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Known spectroscopic and kinetic data are used to formulate pathways of the physiological and transfer reactions and the substrate inhibition of phenol sulfotransferase. Kinetic mechanisms indicate that release of PAP from enzyme complex is required for the physiological reaction but not for the transfer reaction. The pathways explain rate difference between the physiological and transfer reactions since the release of PAP is the rate- limiting step of the former reaction. Two enzyme species of phenol sulfotransferase which distinguish the physiological and transfer reaction were found to involve the binding of PAP. Differences between two forms of phenol sulfotransferase, α and β, indicate that they assemble through different folding process. It is demonstrated that only α enzyme renatures in the presence of PAP and ,β enzyme renatures only in the absence of PAP in vitro. In the over-expressed system, formation of α and β phenol sulfotmnsferase is also dependent on the availability of PAP in Escherichia colt'. It is concluded that folding of phenol sulfotransferase is assisted by PAP to form α enzyme. In the absence of PAP, β form of phenol sulfotransferase is produced.

Original languageEnglish
Pages (from-to)129-135
Number of pages7
JournalChemico-Biological Interactions
Issue number1-3
StatePublished - 20 Feb 1998


  • 3'- phosphoadenosine 5'-phosphate
  • 3'-phosphoadenosine 5'-phosphosulfate
  • Phenol sulfotransferase IV
  • Physiological reaction
  • Protein folding
  • Transfer reaction

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