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Manganese-dependent Dopa/tyrosine sulfation in HepG2 human hepatoma cells: novel Dopa/tyrosine sulfotransferase activities associated with the human monoamine-form phenol sulfotransferase.

Abstract
Human monoamine (M)-form phenol sulfotransferase (PST) was PCR-cloned and transiently expressed in COS-7 cells. The recombinant enzyme was demonstrated to display not only the previously reported sulfotransferase activity toward dopamine, but also novel manganese-dependent Dopa/tyrosine sulfotransferase activities. These results imply a new functional role of the human M-form PST in the homeostatic regulation of Dopa and tyrosine.
AuthorsY Sakakibara, J Katafuchi, Y Takami, T Nakayama, M Suiko, H Nakajima, M C Liu
JournalBiochimica et biophysica acta (Biochim Biophys Acta) Vol. 1355 Issue 2 Pg. 102-6 (Feb 04 1997) ISSN: 0006-3002 [Print] Netherlands
PMID9042329 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Recombinant Proteins
  • Manganese
  • Dopa-tyrosine sulfotransferase
  • Sulfotransferases
  • Arylsulfotransferase
  • Deoxyribonuclease EcoRI
Topics
  • Animals
  • Arylsulfotransferase (metabolism)
  • COS Cells
  • Deoxyribonuclease EcoRI
  • Humans
  • Manganese (metabolism, pharmacology)
  • Recombinant Proteins (metabolism)
  • Sequence Homology, Nucleic Acid
  • Sulfotransferases (metabolism)
  • Tumor Cells, Cultured

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