title: Function and organization of the human cytosolic sulfotransferase (SULT) family.
abstract: The sulfuryl transfer reaction is of fundamental biological importance. One of the most important manifestations of this process are the reactions catalyzed by members of the cytosolic sulfotransferase (SULT) superfamily. These enzymes transfer the sulfuryl moiety from the universal donor PAPS (3'-phosphoadenosine 5'-phosphosulfate) to a wide variety of substrates with hydroxyl- or amino-groups. Normally a detoxification reaction this facilitates the elimination of a multitude of xenobiotics, although for some molecules sulfation is a bioactivation step. In addition, sulfation plays a key role in endocrine and other signalling pathways since many steroids, sterols, thyroid hormones and catecholamines exist primarily as sulfate conjugates in humans. This article summarizes much of our current knowledge of the organization and function of the human cytosolic sulfotransferases and highlights some of the important interspecies differences that have implications for, among other things, drug development and chemical safety analysis.
authors.affiliation: Faculty of Pharmaceutical Sciences, University of British Columbia, 2405 Wesbrook Mall, Vancouver, BC, V6T 1Z3, Canada. Electronic address: michael.coughtrie@ubc.ca.
authors.forename: Michael W H
authors.initials: MWH
authors.lastname: Coughtrie
mesh_terms: D006801:Humans; D008658:Inactivation, Metabolic; D010724:Phosphoadenosine Phosphosulfate / Q000378:metabolism*; D013379:Substrate Specificity; D013431:Sulfates / Q000378:metabolism; D015238:Sulfotransferases / Q000378:metabolism*
chemical_list: D013431:Sulfates; D010724:Phosphoadenosine Phosphosulfate; D015238:Sulfotransferases
keywords: Detoxification; Liver; Metabolism; Sulfation; Sulfotransferase