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Sulfuryl Transfer: The Catalytic Mechanism of Human Estrogen Sulfotransferase
Open accessAbstract
Estrogen sulfotransferase (EST) catalyzes the transfer of the sulfuryl group from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to 17beta-estradiol (E2). The sulfation of E2 prevents it from binding to, and thereby activating, the estrogen receptor. The regulation of EST appears to be causally linked to tumorigenesis in the breast and endometrium. In this study, recombinant human EST is characterized, and the catalytic mechanism of the transfer reaction is investigated in ligand binding and initial rate experiments. The native enzyme is a dimer of 35-kDa subunits. The apparent equilibrium constant for transfer to E2 is (4.5 +/- 0.2) x 10(3) at pH 6.3 and T = 25 +/- 2 degrees C. Initial rate studies provide the kinetic constants for the reaction and suggest a sequential mechanism. E2 is a partial substrate inhibitor (Ki = 80 +/- 5 nM). The binding of two E2 per EST subunit suggests that the partial inhibition occurs through binding at an allosteric site. In addition to providing the dissociation constants for the ligand-enzyme complexes, binding studies demonstrate that each substrate binds independently to the enzyme and that both the E.PAP.E2S and E.PAP.E2 dead-end complexes form. These results strongly suggest a Random Bi Bi mechanism with two dead-end complexes.
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“SULT1E1 is the major SULT for estrogen sulfation [328,329], while SULT1A1 and SULT1A3 also sulfate estrogens, but with a lower affinity [327].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [328]
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On the Distribution of Free-Energy in MetabolismPreprint
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BindingDB Entry 7764: High accuracy in silico sulfotransferase models.
BindingDB (2017) · UC San Diego · doi:10.7270/q2xp73s3
Metadata
- Authors
- Zhang, H., Varmalova, O., Vargas, F. M., Falany, C. N., & Leyh, T. S.
- Affiliations
- Albert Einstein College of Medicine (US)
- University of Alabama at Birmingham (US)
- Corresponding author
- Leyh, Thomas S.
- ORCID
- Leyh, Thomas S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-05
- Volume
- 273
- Issue
- 18
- Pages
- 10888-10892
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1968379731
- Cited by
- 223
- References
- 26
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 5 · 2023: 4 · 2022: 5 · 2021: 5 · 2020: 4 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 7 · 2015: 10 · 2014: 13 · 2013: 12 · 2012: 15
- FWCI
- 3.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (GM54469, GM38953)
- National Institute of General Medical Sciences (GM 54469, R01GM054469, GM-38953)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Physical Sciences › Chemistry › Organic Chemistry › Physical Organic Chemistry and Reaction Kinetics
- Keywords
- estrogen sulfotransferase, PAPS, catalytic mechanism, sequential mechanism, dead-end complex, substrate inhibition, allosteric binding, enzyme kinetics, estrogen receptor, breast cancer, endometrial cancer, enzyme dimer
- MeSH terms
- Catalysis, Cell Line, Chromatography, Gel, Humans, Hydrogen-Ion Concentration, Kinetics, Molecular Weight, Protein Binding, Sulfites, Sulfotransferases
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