ArticleXenobiotica; the fate of foreign compounds in biological systems2018
Oxidation of 1-chloropyrene by human CYP1 family and CYP2A subfamily cytochrome P450 enzymes: catalytic roles of two CYP1B1 and five CYP2A13 allelic variants.
Article in Xenobiotica; the fate of foreign compounds in biological systems, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- CYP1B1- and CYP1A1-Template systems and their application to metabolism and inhibition.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2025Article
- Article
- Preparative Production of Functionalized (Biomolecules · 2022Article
- Roles of cytochrome P450 2A6 in the oxidation of flavone, 4'-hydroxyflavone, and 4'-, 3'-, and 2'-methoxyflavones by human liver microsomes.Xenobiotica; the fate of foreign compounds in biological systems · 2021Article
- The clinical value and potential molecular mechanism of the downregulation of MAOA in hepatocellular carcinoma tissues.Cancer medicine · 2020Article
- Preference forXenobiotica; the fate of foreign compounds in biological systems · 2020Article
- Site-specific oxidation of flavanone and flavone by cytochrome P450 2A6 in human liver microsomes.Xenobiotica; the fate of foreign compounds in biological systems · 2019Article
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Authors and funding
10 authors at 5 institutions in 3 countries.
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Abstract
1. 1-Chloropyrene, one of the major chlorinated polycyclic aromatic hydrocarbon contaminants, was incubated with human cytochrome P450 (P450 or CYP) enzymes including CYP1A1, 1A2, 1B1, 2A6, 2A13, 2B6, 2C9, 2D6, 2E1, 3A4 and 3A5. Catalytic differences in 1-chloropyrene oxidation by polymorphic two CYP1B1 and five CYP2A13 allelic variants were also examined. 2. CYP1A1 oxidized 1-chloropyrene at the 6- and 8-positions more actively than at the 3-position, while both CYP1B1.1 and 1B1.3 preferentially catalyzed 6-hydroxylation. 3. Five CYP2A13 allelic variants oxidized 8-hydroxylation much more than 6- and 3-hydroxylation, and the variant CYP2A13.3 was found to slowly catalyze these reactions with a lower k
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