Sulfation of ritodrine by the human cytosolic sulfotransferases (SULTs): Effects of SULT1A3 genetic polymorphism.
Article Details
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Hui Y, Liu MC
Sulfation of ritodrine by the human cytosolic sulfotransferases (SULTs): Effects of SULT1A3 genetic polymorphism.
Eur J Pharmacol. 2015 Aug 15;761:125-9. doi: 10.1016/j.ejphar.2015.04.039. Epub 2015 May 2.
- PubMed ID
- 25941087 [ View in PubMed]
- Abstract
Previous studies have demonstrated the metabolism of ritodrine through sulfation. The current study was designed to identify the human SULTs that are capable of sulfating ritodrine and to investigate how genetic polymorphism of the major ritodrine-sulfating SULT, SULT1A3, may affect its sulfating activity. A systematic analysis revealed that of the 13 known human SULTs, SULT1A1, SULT1A3, and SULT1C4, were capable of mediating the sulfation of ritodrine, with SULT1A3 displaying the strongest sulfating activity. Effects of genetic polymorphism on the sulfating activity of SULT1A3 were examined. By employing site-directed mutagenesis, 4 SULT1A3 allozymes were generated, expressed, and purified. Purified SULT1A3 allozymes were shown to exhibit differential sulfating activity toward ritodrine. Kinetic studies further demonstrated differential substrate affinity and catalytic efficiency among the SULT1A3 allozymes. Collectively, these results provided useful information concerning the differential metabolism of ritodrine through sulfation in different individuals.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Ritodrine Sulfotransferase 1C4 Protein Humans UnknownSubstrateDetails - Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Ritodrine Sulfotransferase (Protein Group) Protein group Humans NoSubstrateDetails Ritodrine Sulfotransferase 1A1 Protein Humans NoSubstrateDetails Ritodrine Sulfotransferase 1A3/1A4 Protein Humans NoSubstrateDetails Ritodrine Sulfotransferase 1C4 Protein Humans NoSubstrateDetails