Literature DB >> 10503886

Sulfotransferase catalyzing sulfation of heterocyclic amines.

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.

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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


  4 in total

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4.  Structural and Dynamic Characterizations Highlight the Deleterious Role of SULT1A1 R213H Polymorphism in Substrate Binding.

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Journal:  Int J Mol Sci       Date:  2019-12-11       Impact factor: 5.923

  4 in total

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