ArticleBiochemistry2013
The gate that governs sulfotransferase selectivity.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 75 citations in OpenAlex.
- Dock-and-lock binding of SxIP ligands is required for stable and selective EB1 interactions.eLife · 2025Article
- Allosteric Mechanisms Triggering Substrate and Cofactor Binding in the SULT1A1 Dimer as Revealed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025Article
- Sulfotransferase 4A1 Coding Sequence and Protein Structure Are Highly Conserved in Vertebrates.Genes · 2024Review
- A new type of sulfation reaction:PNAS nexus · 2024Article
- Role of Conformational Dynamics of Sulfotransferases SULT1A1 and SULT1A3 in Substrate Specificity.International journal of molecular sciences · 2023Article
- Evaluation of the Toxicity Potential of the Metabolites of Di-Isononyl Phthalate and of Their Interactions with Members of Family 1 of Sulfotransferases-A Computational Study.Molecules (Basel, Switzerland) · 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
- Impact of Human SULT1E1 Polymorphisms on the Sulfation of 17β-Estradiol, 4-Hydroxytamoxifen, and Diethylstilbestrol by SULT1E1 Allozymes.European journal of drug metabolism and pharmacokinetics · 2021Article
- Mechanistic Insights into the Effect of Ligands on Structural Stability and Selectivity of Sulfotransferase 2A1 (SULT2A1).ACS omega · 2019Article
- Effect of SULT2B1 genetic polymorphisms on the sulfation of dehydroepiandrosterone and pregnenolone by SULT2B1b allozymes.Molecular and cellular endocrinology · 2019Article
- Impact of SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of phenylephrine and salbutamol by human SULT1A3 allozymes.Pharmacogenetics and genomics · 2019Article
- Allosteres to regulate neurotransmitter sulfonation.The Journal of biological chemistry · 2019Article
- Isoform-specific therapeutic control of sulfonation in humans.Biochemical pharmacology · 2019Article
- Effects of human SULT1A3/SULT1A4 genetic polymorphisms on the sulfation of acetaminophen and opioid drugs by the cytosolic sulfotransferase SULT1A3.Archives of biochemistry and biophysics · 2018Article
- Sulfation of catecholamines and serotonin by SULT1A3 allozymes.Biochemical pharmacology · 2018Article
- A high frequency missense SULT1B1 allelic variant (L145V) selectively expressed in African descendants exhibits altered kinetic properties.Xenobiotica; the fate of foreign compounds in biological systems · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Human cytosolic sulfotransferases (SULTs) transfer the sulfuryl moiety (-SO(3)) from activated sulfate [3'-phosphoadenosine 5'-phosphosulfate (PAPS)] to the hydroxyls and primary amines of numerous metabolites, drugs, and xenobiotics. Receipt of the sulfuryl group often radically alters acceptor-target interactions. How these enzymes select particular substrates from the hundreds of candidates in a complex cytosol remains an important question. Recent work reveals PAPS binding causes SULT2A1 to undergo an isomerization that controls selectivity by constricting the opening through which acceptors must pass to enter the active site. The enzyme maintains an affinity for large substrates by isomerizing between the open and closed states with nucleotide bound. Here, the molecular basis of the nucleotide-induced closure is explored in equilibrium and nonequilibrium molecular dynamics simulations. The simulations predict that the active-site "cap," which covers both the nucleotide and acceptor binding sites, opens and closes in response to nucleotide. The cap subdivides into nucleotide and acceptor halves whose motions, while coupled, exhibit an independence that can explain the isomerization. In silico weakening of electrostatic interactions between the cap and base of the active site causes the acceptor half of the cap to open and close while the nucleotide lid remains shut. Simulations predict that SULT1A1, the most abundant SULT in human liver, will utilize a similar selection mechanism. This prediction is tested using fulvestrant, an anti-estrogen too large to pass through the closed pore, and estradiol, which is not restricted by closure. Equilibrium and pre-steady-state binding studies confirm that SULT1A1 undergoes a nucleotide-induced isomerzation that controls substrate selection.
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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.