ArticleArchives of biochemistry and biophysics2011
Reaction product affinity regulates activation of human sulfotransferase 1A1 PAP sulfation.
Article in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Advances in Zosteric Acid: Antifouling Properties and Green Biosynthesis Toward Food Safety Applications.Foods (Basel, Switzerland) · 2026Review
- Multi-omics revealed that the postbiotic of hawthorn-probiotic alleviated constipation caused by loperamide in elderly mice.Frontiers in nutrition · 2025Article
- Coelenterazine sulfotransferase from Renilla muelleri.PloS one · 2022Article
- Production of zosteric acid and other sulfated phenolic biochemicals in microbial cell factories.Nature communications · 2019Article
- Preparation of Tyrosylprotein Sulfotransferases for In Vitro One-Pot Enzymatic Synthesis of Sulfated Proteins/Peptides.ACS omega · 2018Article
- Expression, purification and characterization of human cytosolic sulfotransferase (SULT) 1C4.Hormone molecular biology and clinical investigation · 2017Article
- Herb-drug interactions: challenges and opportunities for improved predictions.Drug metabolism and disposition: the biological fate of chemicals · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Cytosolic sulfotransferase (SULT)-catalyzed sulfation regulates the activity of bio-signaling molecules and aids in metabolizing hydroxyl-containing xenobiotics. The sulfuryl donor for the SULT reaction is adenosine 3'-phosphate 5'-phosphosulfate (PAPS), while products are adenosine 3',5'-diphosphate (PAP) and a sulfated alcohol. Human phenol sulfotransferase (SULT1A1) is one of the major detoxifying enzymes for phenolic xenobiotics. The mechanism of SULT1A1-catalyzed sulfation of PAP by pNPS was investigated. PAP was sulfated by para-nitrophenyl sulfate (pNPS) in a concentration-dependent manner. 2-Naphthol inhibited sulfation of PAP, competing with pNPS, while phenol activated the sulfation reaction. At saturating PAP, a ping pong kinetic mechanism is observed with pNPS and phenol as substrates, consistent with phenol intercepting the E-PAPS complex prior to dissociation of PAPS. At high concentrations, phenol competes with pNPS, consistent with formation of the E-PAP-phenol dead-end complex. Data are consistent with the previously reported mechanism for sulfation of 2-naphthol by PAPS, and its activation by pNPS. Overall, data are consistent with release of PAP from E-PAP and PAPS from E-PAPS contributing to rate-limitation in both reaction directions.
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