Evidence map›Paper›PMID 25056952›Full record

ArticleThe Journal of biological chemistry2014

Paradigms of sulfotransferase catalysis: the mechanism of SULT2A1.

Ting Wang, Ian Cook, Charles N Falany, Thomas S Leyh

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. The Human UGT2B7 Nanodisc.Drug metabolism and disposition: the biological fate of chemicals · 2020
    Article
  8. Allosteres to regulate neurotransmitter sulfonation.The Journal of biological chemistry · 2019
    Article
  9. A mechanism for bistability in glycosylation.PLoS computational biology · 2018
    Article
  10. Chalkophores.Annual review of biochemistry · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Design and Interpretation of Human Sulfotransferase 1A1 Assays.Drug metabolism and disposition: the biological fate of chemicals · 2016
    Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Ting WangDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461-1926.
Ian CookDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461-1926.
Charles N FalanyDepartments of Pharmacology and Toxicology, University of Alabama School of Medicine at Birmingham, Birmingham, Alabama 35294-0019 and.
Thomas S LeyhDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York 10461-1926. Electronic address: tom.leyh@einstein.yu.edu.
Albert Einstein College of Medicine · USUniversity of Alabama at Birmingham · US

Funding

SULFATE ADENYLATION-BIOCHEMISTRY &ENZYMOLOGYR01GM054469 · NIGMS · YESHIVA UNIVERSITY · PI LEYH, THOMAS S. · 1995 to 2011
$4.7M
HUMAN CYTOSOLIC SULFOTRANSFERASESR01GM038953 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FALANY, CHARLES N · 1992 to 2013
$3.3M
Sulfotransferase Specificity and the Development of Sulfation Resistant CompoundsR01GM106158 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI LEYH, THOMAS S. · 2014 to 2016
$1.1M
HUMAN PLATELET PHENOL SULFOTRANSFERASESR29GM038953 · NIGMS · UNIVERSITY OF ROCHESTER · PI FALANY, CHARLES N · 1987 to 1991
–
NIGMS NIH HHS GM38953NIGMS NIH HHS GM54469NIGMS NIH HHS R01 GM038953NIGMS NIH HHS R01 GM054469NIGMS NIH HHS R01 GM106158
6 · The paper itself

Abstract

Human cytosolic sulfotransferases (SULTs) regulate the activities of thousands of signaling small molecules via transfer of the sulfuryl moiety (-SO3) from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the hydroxyls and primary amines of acceptors. Sulfonation controls the affinities of ligands for their targets, and thereby regulates numerous receptors, which, in turn, regulate complex cellular responses. Despite their biological and medical relevance, basic SULT mechanism issues remain unresolved. To settle these issues, and to create an in-depth model of SULT catalysis, the complete kinetic mechanism of a representative member of the human SULT family, SULT2A1, was determined. The mechanism is composed of eight enzyme forms that interconvert via 22 rate constants, each of which was determined independently. The result is a complete quantitative description of the mechanism that accurately predicts complex enzymatic behavior. This is the first description of a SULT mechanism at this resolution, and it reveals numerous principles of SULT catalysis and resolves previously ambiguous issues. The structures and catalytic behaviors SULTs are highly conserved; hence, the mechanism presented here should prove paradigmatic for the family.

Indexed as

BiocatalysisDehydroepiandrosteroneHumansKineticsModels, ChemicalPhosphoadenosine PhosphosulfateProtein BindingSulfotransferasesalcohol sulfotransferaseDehydroepiandrosteronePhosphoadenosine PhosphosulfateSulfotransferasesDHEAEnzyme MechanismLigand-binding proteinMetabolic RegulationMetabolismPre-steady StateRate ConstantSubstrate InhibitionSulfotransferaseSULT2A1

Identifiers

PMID25056952
PMCPMC4176245
OpenAlexW2047842825

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.