Sulfotransferase catalyzing sulfation of heterocyclic amines

Cancer Lett. 1999 Sep 1;143(2):103-7. doi: 10.1016/s0304-3835(99)00136-6.


Cytosolic sulfation of arylamines to form sulfamates is found to be mediated by sulfotransferases of three gene families (SULT1 to 3). Among them, a SULT3 form (ST3A1) showed a high selectivity for N-sulfation of N-substituted aryl and alicyclic compounds. SULT1 (phenol) and SULT2 (hydroxysteroid) sulfotransferases showed N-sulfating activities of carcinogenic heterocyclic amines. For N-hydroxyarylamine O-sulfation, SULT1 forms showed high activity. In rats, ST1C1 mediated the metabolic activation of N-hydroxyarylamines. However, the related form (ST1C2) in humans showed the negligible activity. Instead, ST1A3 showed high metabolic activating abilities among human sulfotransferases.

MeSH terms

  • Amines / metabolism*
  • Amino Acid Sequence
  • Animals
  • Catalysis
  • Enzyme Activation
  • Humans
  • Molecular Sequence Data
  • Rats
  • Sequence Alignment
  • Substrate Specificity
  • Sulfotransferases / metabolism*


  • Amines
  • Sulfotransferases