Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects

Mutat Res. 2001 Oct 1;482(1-2):27-40. doi: 10.1016/s0027-5107(01)00207-x.


Cytosolic sulphotransferases transfer the sulpho moiety from the cofactor 5'-phosphoadenosine-3'-phosphosulphate (PAPS) to nucleophilic groups of xenobiotics and small endogenous compounds (such as hormones and neurotransmitters). This reaction often leads to products that can be excreted readily. However, other sulpho conjugates are strong electrophiles and may covalently bind with DNA and proteins. All known cytosolic sulphotransferases are members of an enzyme/gene superfamily termed SULT. In humans, 10 SULT genes are known. One of these genes encodes two different enzyme forms due to the use of alternative first exons. Different SULT forms substantially differ in their substrate specificity and tissue distribution. Genetic polymorphisms have been described for three human SULTs. Several allelic variants differ in functional properties, including the activation of promutagens. Only initial results are available from the analysis of SULT allele frequencies in different population groups, e.g. subjects suffering from specific diseases and corresponding controls.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Arylsulfotransferase*
  • Cytosol / enzymology*
  • Genetics, Population*
  • Humans
  • Inactivation, Metabolic
  • Substrate Specificity
  • Sulfotransferases / genetics*
  • Sulfotransferases / metabolism*
  • Terminology as Topic
  • Xenobiotics* / metabolism


  • Xenobiotics
  • Dopa-tyrosine sulfotransferase
  • Sulfotransferases
  • Arylsulfotransferase
  • SULT1A1 protein, human
  • monoamine-sulfating phenol sulfotransferase
  • SULT2B1 protein, human