Sulfotransferase catalyzing sulfation of heterocyclic amines.
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.
Yamazoe
Y
Y
Division of Drug Metabolism and Molecular Toxicology, Faculty of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Nagata
K
K
Yoshinari
K
K
Fujita
K
K
Shiraga
T
T
Iwasaki
K
K
D000588:Amines / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002384:Catalysis; D004789:Enzyme Activation; D006801:Humans; D008969:Molecular Sequence Data; D051381:Rats; D016415:Sequence Alignment; D013379:Substrate Specificity; D015238:Sulfotransferases / Q000378:metabolism*
D000588:Amines; D015238:Sulfotransferases