Crystal structure-based studies of cytosolic sulfotransferase

Kouichi Yoshinari, Evgeniy V. Petrotchenko, Lars C. Pedersen, Masahiko Negishi

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Sulfation is a widely observed biological reaction conserved from bacterium to human that plays a key role in various biological processes such as growth, development, and defense against adversities. Deficiencies due to the lack of the ubiquitous sulfate donor 3′-phosphoadenosine-5′-phosphosulfate (PAPS) are lethal in humans. A large group of enzymes called sulfotransferases catalyze the transfer reaction of sulfuryl group of PAPS to the acceptor group of numerous biochemical and xenochemical substrates. Four X-ray crystal structures of sulfotransferases have now been determined: cytosolic estrogen, hydroxysteroid, aryl sulfotransferases, and a sulfotransferase domain of the Golgi-membrane heparan sulfate N-deacetylase/N-sulfotransferase 1. These have revealed the conserved core structure of the PAPS binding site, a common reaction mechanism, and some information concerning the substrate specificity. These crystal structures introduce a new era of the study of the sulfotransferases.

Original languageEnglish
Pages (from-to)67-75
Number of pages9
JournalJournal of Biochemical and Molecular Toxicology
Volume15
Issue number2
DOIs
Publication statusPublished - 2001 Apr 30

Keywords

  • 3′-phosphoadenosine-5′-phosphosulfate
  • Sulfation
  • Sulfotransferases
  • X-ray crystal structures

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Toxicology
  • Health, Toxicology and Mutagenesis

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  • Cite this

    Yoshinari, K., Petrotchenko, E. V., Pedersen, L. C., & Negishi, M. (2001). Crystal structure-based studies of cytosolic sulfotransferase. Journal of Biochemical and Molecular Toxicology, 15(2), 67-75. https://doi.org/10.1002/jbt.1