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http://purl.uniprot.org/citations/12865317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12865317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12865317http://www.w3.org/2000/01/rdf-schema#comment"We systematically characterized the oxidative metabolites of 17beta-estradiol and estrone formed by 15 human cytochrome P450 (CYP) isoforms. CYP1A1 had high activity for 17beta-estradiol 2-hydroxylation, followed by 15alpha-, 6alpha-, 4-, and 7alpha-hydroxylation. However, when estrone was the substrate, CYP1A1 formed more 4-hydroxyestrone than 15alpha- or 6alpha-hydroxyestrone, with 2-hydroxyestrone as the major metabolite. CYP1A2 had the highest activity for the 2-hydroxylation of both 17beta-estradiol and estrone, although it also had considerable activity for their 4-hydroxylation (9-13% of 2-hydroxylation). CYP1B1 mainly catalyzed the formation of catechol estrogens, with 4-hydroxyestrogens predominant. CYP2A6, 2B6, 2C8, 2C9, 2C19, and 2D6 each showed a varying degree of low catalytic activity for estrogen 2-hydroxylation, whereas CYP2C18 and CYP2E1 did not show any detectable estrogen-hydroxylating activity. CYP3A4 had strong activity for the formation of 2-hydroxyestradiol, followed by 4-hydroxyestradiol and an unknown polar metabolite, and small amounts of 16alpha- and 16beta-hydroxyestrogens were also formed. The ratio of 4-to 2-hydroxylation of 17beta-estradiol or estrone with CYP3A4 was 0.22 or 0.51, respectively. CYP3A5 had similar catalytic activity for the formation of 2- and 4- hydroxyestrogens. Notably, CYP3A5 had an unusually high ratio of 4-to 2-hydroxylation of 17beta-estradiol or estrone (0.53 or 1.26, respectively). CYP3A4 and 3A5 also catalyzed the formation of nonpolar estrogen metabolite peaks (chromatographically less polar than estrone). CYP3A7 had a distinct catalytic activity for the 16alpha-hydroxylation of estrone, but not 17beta-estradiol. CYP4A11 had little catalytic activity for the metabolism of 17beta-estradiol and estrone. In conclusion, many human CYP isoforms are involved in the oxidative metabolism of 17beta-estradiol and estrone, with a varying degree of catalytic activity and distinct regioselectivity."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.org/dc/terms/identifier"doi:10.1210/en.2003-0192"xsd:string
http://purl.uniprot.org/citations/12865317http://purl.org/dc/terms/identifier"doi:10.1210/en.2003-0192"xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Thomas P.E."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Thomas P.E."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Lee A.J."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Lee A.J."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Cai M.X."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Cai M.X."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Conney A.H."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Conney A.H."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Zhu B.T."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/author"Zhu B.T."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/name"Endocrinology"xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/name"Endocrinology"xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/pages"3382-3398"xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/pages"3382-3398"xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/title"Characterization of the oxidative metabolites of 17beta-estradiol and estrone formed by 15 selectively expressed human cytochrome p450 isoforms."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/title"Characterization of the oxidative metabolites of 17beta-estradiol and estrone formed by 15 selectively expressed human cytochrome p450 isoforms."xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/volume"144"xsd:string
http://purl.uniprot.org/citations/12865317http://purl.uniprot.org/core/volume"144"xsd:string
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