ArticleBiochemistry2014
3'-Phosphoadenosine 5'-phosphosulfate allosterically regulates sulfotransferase turnover.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Allosteric Mechanisms Triggering Substrate and Cofactor Binding in the SULT1A1 Dimer as Revealed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025Article
- Review
- Complex roles for sulfation in the toxicities of polychlorinated biphenyls.Critical reviews in toxicology · 2024Review
- 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
- Article
- 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
- Human DHEA sulfation requires direct interaction between PAPS synthase 2 and DHEA sulfotransferase SULT2A1.The Journal of biological chemistry · 2018Article
- 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
- Expression, purification and characterization of human cytosolic sulfotransferase (SULT) 1C4.Hormone molecular biology and clinical investigation · 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
- An engineered heterodimeric model to investigate SULT1B1 dependence on intersubunit communication.Biochemical pharmacology · 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
- In Silico Prediction of Human Sulfotransferase 1E1 Activity Guided by Pharmacophores from Molecular Dynamics Simulations.The Journal of biological chemistry · 2016Article
- 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
3 authors at 1 institution in 1 country.
Funding
Abstract
Human cytosolic sulfotransferases (SULTs) regulate the activities of thousands of small molecules-metabolites, drugs, and other xenobiotics-via the transfer of the sulfuryl moiety (-SO3) from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the hydroxyls and primary amines of acceptors. SULT1A1 is the most abundant SULT in liver and has the broadest substrate spectrum of any SULT. Here we present the discovery of a new form of SULT1A1 allosteric regulation that modulates the catalytic efficiency of the enzyme over a 130-fold dynamic range. The molecular basis of the regulation is explored in detail and is shown to be rooted in an energetic coupling between the active-site caps of adjacent subunits in the SULT1A1 dimer. The first nucleotide to bind causes closure of the cap to which it is bound and at the same time stabilizes the cap in the adjacent subunit in the open position. Binding of the second nucleotide causes both caps to open. Cap closure sterically controls active-site access of the nucleotide and acceptor; consequently, the structural changes in the cap that occur as a function of nucleotide occupancy lead to changes in the substrate affinities and turnover of the enzyme. PAPS levels in tissues from a variety of organs suggest that the catalytic efficiency of the enzyme varies across tissues over the full 130-fold range and that efficiency is greatest in those tissues that experience the greatest xenobiotic "load".
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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.