ArticleDrug metabolism and disposition: the biological fate of chemicals2016
Catalytic Activities of Tumor-Specific Human Cytochrome P450 CYP2W1 Toward Endogenous Substrates.
Article in Drug metabolism and disposition: the biological fate of chemicals, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
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- Orphan Cytochromes P450 as Possible Pharmacological Targets or Biomarkers in Breast Cancer.Current issues in molecular biology · 2025Review
- CYP2S1 and CYP2W1 expression is associated with patient survival in breast cancer.The journal of pathology. Clinical research · 2022Article
- Human Orphan Cytochromes P450: An Update.Current drug metabolism · 2022Article
- Cytochrome P450 Binding and Bioactivation of Tumor-Targeted Duocarmycin Agents.Drug metabolism and disposition: the biological fate of chemicals · 2022Article
- Cytochrome P450 isoforms 1A1, 1B1 AND 2W1 as targets for therapeutic intervention in head and neck cancer.Scientific reports · 2021Article
- Intratumoural Cytochrome P450 Expression in Breast Cancer: Impact on Standard of Care Treatment and New Efforts to Develop Tumour-Selective Therapies.Biomedicines · 2021Review
- Human Family 1-4 cytochrome P450 enzymes involved in the metabolic activation of xenobiotic and physiological chemicals: an update.Archives of toxicology · 2021Review
- Potential role of gut microbiota, the proto-oncogene PIKE (Agap2) and cytochrome P450 CYP2W1 in promotion of liver cancer by alcoholic and nonalcoholic fatty liver disease and protection by dietary soy protein.Chemico-biological interactions · 2020Article
- Protein Encapsulation of Experimental Anticancer Agents 5F 203 and Phortress: Towards Precision Drug Delivery.International journal of nanomedicine · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
CYP2W1 is a recently discovered human cytochrome P450 enzyme with a distinctive tumor-specific expression pattern. We show here that CYP2W1 exhibits tight binding affinities for retinoids, which have low nanomolar binding constants, and much poorer binding constants in the micromolar range for four other ligands. CYP2W1 converts all-transretinoic acid (atRA) to 4-hydroxyatRA and all-transretinol to 4-OH all-transretinol, and it also oxidizes retinal. The enzyme much less efficiently oxidizes 17β-estradiol to 2-hydroxy-(17β)-estradiol and farnesol to a monohydroxylated product; arachidonic acid is, at best, a negligible substrate. These findings indicate that CYP2W1 probably plays an important role in localized retinoid metabolism that may be intimately linked to its involvement in tumor development.
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