Mechanism and inhibition of cytochrome P-450 aromatase
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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTMechanism and inhibition of cytochrome P-450 aromatasePhilip A. Cole and Cecil H. RobinsonCite this: J. Med. Chem. 1990, 33, 11, 2933–2942Publication Date (Print):November 1, 1990Publication History Published online1 May 2002Published inissue 1 November 1990https://pubs.acs.org/doi/10.1021/jm00173a001https://doi.org/10.1021/jm00173a001research-articleACS PublicationsRequest reuse permissionsArticle Views691Altmetric-Citations263LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
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Aromatase catalyzes the rate-limiting final step in estrogen production, the hydroxylation of androstenedione to estrone and of T to E2.
“It catalyzes the rate-limiting final step in estrogen (E) production, the hydroxylation of androstenedione to estrone and of T to E 2 (Fig. 1).”
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“In post-menopausal women, the main source of estrogens is the adipose tissue (Cole and Robinson, 1990).”
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“Aromatase is a microsomal member of the cytochrome P450 haemoprotein-containing enzyme complex superfamily (P450arom, the product of the CYP19 gene) that catalyses the rate-limiting step in the production of oestrogens, that is, the conversion of androstenedione and testosterone via three hydroxylation steps to estron…”
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“Aromatase is a cytochrome P450 enzyme complex that catalyzes the conversion of androstenedione and testosterone to their respective estrogenic products estrone and E2 (42).”
BackgroundMiller, W. R., Bartlett, J. M. S., Brodie, A. M. H., Brueggemeier, R. W., di Salle, E., Lønning, P. E., Llombart‐Cussac, A., Maass, N., Maudelondé, T., Sasano, H., et al. (2008) · The Oncologist · doi:10.1634/theoncologist.2008-0055 · Cited by 117 · see citing works
“Aromatase is a member of the cytochrome P450 (CYP)19 familyofenzymes[8–10].NonsteroidaltypeIIAIs,suchas anastrozole and letrozole, interact noncovalently with the heme moiety of aromatase and occupy its substrate-binding site, thereby preventing binding of androgens to the catalytic site [ 11 ] (Fig. 2). This antagoni…”
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“The majority of circulating estrogens in premenopausal women is in the form of E2 and is produced cyclically by the granulosa cells of the ovarian follicles ( 39 ).”
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“Most of the efforts involving synthetic organic chemistry were carried out earlier and are well accounted for in the review by Cole and Robinson.21 However, a recent finding by Wertz et al.97 might be worth mentioning here.”
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“Introduction Aromatase is a microsomal member of the cytochrome P450 hemoprotein-containing enzyme complex superfamily (P450arom, the product of the CYP19 gene) that catalyzes the rate-limiting step in the production of estrogens; that is, the conversion of androstenedione and testosterone via three hydroxylation step…”
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“Aromatase, a member of the cytochrome P450 superfamily, is the enzyme catalyzing the rate-limiting step in the biosynthesis of estrogens [38].”
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“The conversion of androgens (testosterone and androstenedione) to estrogens (estradiol and estrone) by aromatase is an unique reaction in steroidogenesis and the final, rate-limiting step in estrogen biosynthesis [3].”
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- Authors
- Cole, P. A., & Robinson, C. H.
- Affiliations
- Johns Hopkins University (US)
- ORCID
- Cole, Philip A.
- Venue
- Journal of Medicinal Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1990-11
- Volume
- 33
- Issue
- 11
- Pages
- 2933-2942
- ISSN
- 0022-2623 (ISSN-L)
- 1520-4804
- OpenAlex
- W1978841200
- Cited by
- 319
- References
- 0
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 4 · 2023: 6 · 2022: 4 · 2021: 7 · 2020: 5 · 2019: 3 · 2018: 4 · 2017: 35 · 2016: 5 · 2015: 32 · 2014: 6 · 2013: 5 · 2012: 12
- FWCI
- 6.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01hd011840-15)
- National Institute of General Medical Sciences (T32GM007309, GM07309)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD11840)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Keywords
- enzyme mechanism, enzyme inhibition, aromatase inhibitors, steroidogenesis
- MeSH terms
- Affinity Labels, Aromatase, Binding, Competitive, Humans, Photochemistry, Molecular Structure, Aromatase Inhibitors
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