A prototype of the mammalian sulfotransferase 1 (SULT1) family in Xenopus laevis : molecular and enzymatic properties of XlSULT1B.S

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  • Yamauchi Kiyoshi
    Department of Biological Science, Faculty of Science, Shizuoka University
  • Katsumata Shinpei
    Department of Biological Science, Faculty of Science, Shizuoka University
  • Ozaki Masanao
    Department of Biological Science, Faculty of Science, Shizuoka University

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  • A prototype of the mammalian sulfotransferase 1 (SULT1) family in <i>Xenopus laevis</i>: molecular and enzymatic properties of <i>Xl</i>SULT1B.S

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<p>The cytosolic sulfotransferase 1 (SULT1) proteins are a family of highly divergent proteins that show variable expansion in different species during vertebrate evolution. To clarify the evolutionary origin of the mammalian lineage of the SULT1 family, we compiled Xenopus laevis and X. tropicalis SULT1 (XSULT1) sequences from public databases. The XSULT1 family was found to comprise at least six subfamilies, which corresponded in part to five mammalian SULT1 subfamilies but only poorly to zebrafish SULT1 subfamilies. SULT1C was most highly expanded, and could be divided into at least five subfamilies. A cDNA for X. laevis SULT1B (XlSULT1B.S), a homolog of mammalian SULT1B1, was cloned and its recombinant protein was expressed in a bacterial system. XlSULT1B.S, unlike mammalian SULT1B1, was found to be a monomeric protein of ~34 kDa, and displayed sulfonating activity toward 2-naphthol and p-nitrophenol (pNP). However, we could not detect such sulfonating activity toward any endogenous compounds including thyroid hormones, steroid hormones and dopamine, despite the fact that X. laevis and Rana catesbeiana liver cytosols contained sulfonating activity toward most of these endogenous compounds. At optimum pH (6.4), the Michaelis–Menten constant (Km) for pNP was two orders of magnitude greater in XlSULT1B.S (1.04 mM) than in the cytosol preparations (8–15 μM). Our results indicate that Xenopus possesses a prototype of the mammalian SULT1 family, and that XlSULT1B.S showed overall similarities in primary sequence to, and significant differences in molecular and enzymatic properties from, mammalian SULT1B1.</p>

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