Steroid sulfotransferases
Abstract
THE discovery that steroids are excreted in urine as conjugates of sulfuric acid was made more than 50 yr ago (1, 2). The enzymes responsible for forming the steroid sulfoconjugates, however, were not initially examined until almost 20 yr later (3–6). After that, interest rose rapidly, resulting in considerable progress for this important and intriguing metabolic process. The importance pertains to the striking change in the physical, chemical, and biological properties that occurs on formation of steroid sulfoconjugates; the fascination relates to the fact that the biological significance of this process, for the most part, remains a conundrum. It is especially enigmatic in steroidogenic tissues such as the adrenal, ovary, and testis. The fact is, 40 yr of investigation, notwithstanding, neither the biochemistry nor the biological import of steroid sulfonation is well understood. The enzymology, although appearing simple in principle, is complex and although interesting functional implications have been put forth, the biology of steroid sulfonation has been difficult to assess and thus remains largely speculative.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Tissue estrogen sulfotransferase is a critical mediator of estrogen action; it inhibits estrogen activity by conjugating a sulfonate group to estrogens, preventing binding to estrogen receptors.
“Tissue estrogen sulfotransferase (EST) is a critical mediator of estrogen action. EST inhibits estrogen activity by conjugating a sulfonate group to estrogens, thereby preventing biding to estrogen receptors [126].”
From Estrogen deficiency and the origin of obesity during menopause (2014) · cites this paper as [126]
SULT2A2 can target 3α- and 17β-hydroxyl groups and has been shown to sulfate An, testosterone and DHT.
“SULT2A2 can target 3α- and 17β-hydroxyl groups and has been shown to sulfate An, testosterone and DHT [294,295].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [294]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
The citation lists haven’t been fetched yet
References 128 · Cited by 200
Research works printed but not linked: 7
- Roy AB 1981 Sulfotransferases In: Mulder GJ (ed) Sulfation of Drugs and Related Compounds. CRC Press, Boca Raton, FL, pp 83-130
- Mulder GJ, Jakoby WB 1990 Sulfation. In: Mulder GJ (ed) Con- jugation Reactions in Drug Metabolism. Taylor & Francis, New York, pp 107-161
- Huxtable RJ1986 Biochemistry of Sulfur. Plenum Press, New York, pp 293-358
- Weinshilboum R, Otterness D 1994 Sulfotransferase enzymes. In: Kauffman FC (ed) Conjugation-Deconjugation Reactions in Drug Metabolism and Toxicity. Handbook of Experimental Pharmacol- ogy. Springer-Verlag, New York, vol 112:45-78
- Webb EC (ed) 1992 Enzyme Nomenclature. Academic Press, New York, pp 299-303
- Mulder GJ 1981 Sulfate activation. In: Mulder GJ (ed) Sulfation of Drugs and Related Compounds. CRC Press, Boca Raton, FL, pp 70-73
- Roberts KD, Lieberman S 1970 The biochemistry of the 3/3-hy- droxy-A 5 -steroid sulfates. In: Bernstein S, Solomon S (eds) Chem- ical and Biological Aspects of Steroid Conjugation. Springer- Verlag, New York, pp 219-290 203.
- Authors
- STROTT, C. A.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- STROTT, CHARLES A.
- Venue
- Endocrine Reviews
- Publisher
- The Endocrine Society
- Published
- 1996-12
- Volume
- 17
- Issue
- 6
- Pages
- 670-697
- ISSN
- 0163-769X (ISSN-L)
- 1945-7189
- OpenAlex
- W4235559323
- Cited by
- 200
- References
- 128
- Citations by year
- 2025: 3 · 2024: 3 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 3 · 2018: 8 · 2017: 14 · 2016: 5 · 2015: 7 · 2014: 5 · 2013: 5 · 2012: 4
- FWCI
- 11.29
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Endocrine Reviews (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Keywords
- steroid metabolism, steroid excretion, steroidogenic tissues, adrenal gland, ovary, testis, enzyme biochemistry
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Humans, Molecular Sequence Data, Steroids, Sulfotransferases, Sequence Alignment
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review