Reactome: A Curated Pathway Database

Cytosolic sulfonation of small molecules

Stable Identifier
Homo sapiens
Locations in the PathwayBrowser

Two groups of sulfotransferease (SULT) enzymes catalyze the transfer of a sulfate group from 3-phosphoadenosine 5-phosphosulfate (PAPS) to a hydroxyl group on an acceptor molecule, yielding a sulfonated acceptor and 3-phosphoadenosine 5-phosphate (PAP). One is localized to the Golgi apparatus and mediates the sulfonation of proteoglycans. The second, annotated here, is cytosolic and mediates the sulfonation of a diverse array of small molecules, increasing their solubilities in water and modifying their physiological functions. There are probably thirteen or more human cytosolic SULT enzymes; eleven of these have been purified and characterized enzymatically, and are annotated here (Blanchard et al. 2004; Gamage et al. 2005). These enzymes appear to be active as dimers. Their substrate specificities are typically broad, and not related in an obvious way to their structures; indeed, apparently orthologous human and rodent SULT enzymes can have different substrate specificities (Glatt 2000), and none has been exhaustively characterized. The substrates listed in the table and annotated here are a sample of the known ones, chosen to indicate the range of activity of these enzymes and to capture some of their known physiologically important targets. Absence of a small molecule - enzyme pair from the table, however, may only mean that it has not yet been studied.

Literature References
PubMed ID Title Journal Year
12372849 Sulfonation and molecular action Endocr Rev 2002
10503886 Sulfotransferase catalyzing sulfation of heterocyclic amines Cancer Lett 1999
  Casarett and Doull's Toxicology 5th Edn   1995
9034160 Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes FASEB J 1997
Participant Of
Orthologous Events