ArticleDrug metabolism and disposition: the biological fate of chemicals2015
The allosteric binding sites of sulfotransferase 1A1.
Article in Drug metabolism and disposition: the biological fate of chemicals, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03383133 (Allosteric Regulation of Cytosolic Sulfotransferases in Humans), which is not on this map. Cited by 17 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Allosteric Regulation of Cytosolic Sulfotransferases in Humans
Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Cytosolic sulfotransferases in endocrine disruption.Essays in biochemistry · 2024Review
- Complex roles for sulfation in the toxicities of polychlorinated biphenyls.Critical reviews in toxicology · 2024Review
- Role of Conformational Dynamics of Sulfotransferases SULT1A1 and SULT1A3 in Substrate Specificity.International journal of molecular sciences · 2023Article
- Sulfotransferase 2B1b, Sterol Sulfonation, and Disease.Pharmacological reviews · 2023Review
- From Steroid and Drug Metabolism to Glycobiology, Using Sulfotransferase Structures to Understand and Tailor Function.Drug metabolism and disposition: the biological fate of chemicals · 2022Review
- Computational Analysis of Chemical Space of Natural Compounds Interacting with Sulfotransferases.Molecules (Basel, Switzerland) · 2021Article
- Insights into the substrate binding mechanism of SULT1A1 through molecular dynamics with excited normal modes simulations.Scientific reports · 2021Article
- Enzyme Kinetics of PAPS-Sulfotransferase.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Allosteres to regulate neurotransmitter sulfonation.The Journal of biological chemistry · 2019Article
- Isoform-specific therapeutic control of sulfonation in humans.Biochemical pharmacology · 2019Article
- The NSAID allosteric site of human cytosolic sulfotransferases.The Journal of biological chemistry · 2017Article
- Tetrahydrobiopterin regulates monoamine neurotransmitter sulfonation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The structure of the catechin-binding site of human sulfotransferase 1A1.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1.Biochemistry · 2016Article
- Design and Interpretation of Human Sulfotransferase 1A1 Assays.Drug metabolism and disposition: the biological fate of chemicals · 2016Review
- Sulfotransferase 1A1 Substrate Selectivity: A Molecular Clamp Mechanism.Biochemistry · 2015Article
- Small-molecule control of neurotransmitter sulfonation.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Human sulfotransferases (SULTs) comprise a small, 13-member enzyme family that regulates the activities of thousands of compounds-endogenous metabolites, drugs, and other xenobiotics. SULTs transfer the sulfuryl-moiety (-SO3) from a nucleotide donor, PAPS (3'-phosphoadenosine 5'-phosphosulfate), to the hydroxyls and primary amines of acceptors. SULT1A1, a progenitor of the family, has evolved to sulfonate compounds that are remarkably structurally diverse. SULT1A1, which is found in many tissues, is the predominant SULT in liver, where it is a major component of phase II metabolism. Early work demonstrated that catechins and nonsteroidal anti-inflammatory drugs inhibit SULT1A1 and suggested that the inhibition was not competitive versus substrates. Here, the mechanism of inhibition of a single, high affinity representative from each class [epigallocatechin gallate (EGCG) and mefenamic acid] is determined using initial-rate and equilibrium-binding studies. The findings reveal that the inhibitors bind at sites separate from those of substrates, and at saturation turnover of the enzyme is reduced to a nonzero value. Further, the EGCG inhibition patterns suggest a molecular explanation for its isozyme specificity. Remarkably, the inhibitors bind at sites that are separate from one another, and binding at one site does not affect affinity at the other. For the first time, it is clear that SULT1A1 is allosterically regulated, and that it contains at least two, functionally distinct allosteric sites, each of which responds to a different class of compounds.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.