Sulfotransferase 4A1

Int J Biochem Cell Biol. 2008;40(12):2686-91. doi: 10.1016/j.biocel.2007.11.010. Epub 2007 Dec 3.


In this review, we highlight the physical and enzymatic properties of the novel human sulfotransferase, SULT4A1. The gene is most highly expressed in selective regions of the brain, although work to date has failed to identify any specific endogenous substrate for the enzyme. SULT4A1 shares low homology with other human sulfotransferases. Nevertheless, it is highly conserved between species. Despite the low homology, it is structurally very similar to other cytosolic sulfotransferases with a conserved substrate binding domain, dimerization site and partial cofactor binding sites. However, the catalytic cavity is much smaller, and it has been suggested that the cofactor may not be accommodated within it. A recent link between variability in the 5'UTR of the SULT4A1 gene and schizophrenia has heightened interest in the endogenous function of the enzyme and its possible role in human disease.

Publication types

  • Review

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Binding Sites
  • Cloning, Molecular
  • Cytosol / enzymology
  • Cytosol / metabolism
  • DNA, Complementary / genetics
  • DNA, Complementary / metabolism
  • Dimerization
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Sulfotransferases / chemistry*
  • Sulfotransferases / genetics
  • Sulfotransferases / metabolism*


  • DNA, Complementary
  • SULT4A1 protein, human
  • Sulfotransferases