| Literature DB >> 10503886 |
Y Yamazoe1, K Nagata, K Yoshinari, K Fujita, T Shiraga, K Iwasaki.
Abstract
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.Entities:
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Year: 1999 PMID: 10503886 DOI: 10.1016/s0304-3835(99)00136-6
Source DB: PubMed Journal: Cancer Lett ISSN: 0304-3835 Impact factor: 8.679