Sulphation of acetaminophen by the human cytosolic sulfotransferases: a systematic analysis.
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Yamamoto A, Liu MY, Kurogi K, Sakakibara Y, Saeki Y, Suiko M, Liu MC
Sulphation of acetaminophen by the human cytosolic sulfotransferases: a systematic analysis.
J Biochem. 2015 Dec;158(6):497-504. doi: 10.1093/jb/mvv062. Epub 2015 Jun 11.
- PubMed ID
- 26067475 [ View in PubMed]
- Abstract
Sulphation is known to be critically involved in the metabolism of acetaminophen in vivo. This study aimed to systematically identify the major human cytosolic sulfotransferase (SULT) enzyme(s) responsible for the sulphation of acetaminophen. A systematic analysis showed that three of the twelve human SULTs, SULT1A1, SULT1A3 and SULT1C4, displayed the strongest sulphating activity towards acetaminophen. The pH dependence of the sulphation of acetaminophen by each of these three SULTs was examined. Kinetic parameters of these three SULTs in catalysing acetaminophen sulphation were determined. Moreover, sulphation of acetaminophen was shown to occur in HepG2 human hepatoma cells and Caco-2 human intestinal epithelial cells under the metabolic setting. Of the four human organ samples tested, liver and intestine cytosols displayed considerably higher acetaminophen-sulphating activity than those of lung and kidney. Collectively, these results provided useful information concerning the biochemical basis underlying the metabolism of acetaminophen in vivo previously reported.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Acetaminophen Sulfotransferase 1A1 Protein Humans UnknownSubstrateDetails Acetaminophen Sulfotransferase 1A3/1A4 Protein Humans UnknownSubstrateDetails