Sulfotransferases: Structure, mechanism, biological activity, inhibition, and synthetic utility

Eli Chapman, Michael D. Best, Sarah R. Hanson, Chi Huey Wong

Research output: Contribution to journalReview article

204 Scopus citations

Abstract

The sulfonation (also known as sulfurylation) of biomolecules has long been known to take place in a variety of organisms, from prokaryotes to multicellular species, and new biological functions continue to be uncovered in connection with this important transformation. Early studies of sulfotransferases (STs), the enzymes that catalyze sulfonation, focused primarily on the cytosolic STs, which are involved in detoxification, hormone regulation, and drug metabolism. Although known to exist, the membrane-associated STs were not studied as extensively until more recently. Involved in the sulfonation of complex carbohydrates and proteins, they have emerged as central players in a number of molecular-recognition events and biochemical signaling pathways. STs have also been implicated in many pathophysiological processes. As a result, much interest in the complex roles of STs and in their targeting for therapeutic intervention has been generated. Progress in the elucidation of the structures and mechanisms of sulfotransferases, as well as their biological activity, inhibition, and synthetic utility, are discussed in this Review.

Original languageEnglish (US)
Pages (from-to)3526-3548
Number of pages23
JournalAngewandte Chemie - International Edition
Volume43
Issue number27
DOIs
StatePublished - Jul 5 2004
Externally publishedYes

Keywords

  • Biological activity
  • Combinatorial chemistry
  • Enzymes
  • Inhibitors
  • Sulfotransferases

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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