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http://purl.uniprot.org/citations/7690968http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7690968http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7690968http://www.w3.org/2000/01/rdf-schema#comment"A full-length cDNA for the human liver mitochondrial cytochrome P-450 CYP27 was cloned from a human hepatoma HepG2 cDNA library and then subcloned into the mammalian expression vector pSG5. When CYP27 cDNA was transfected into COS-1 transformed monkey kidney cells along with adrenodoxin cDNA, transfected cells revealed a 10-to 20-fold higher vitamin D3-25-hydroxylase activity than nontransfected cells. Transfected cells were capable of 25-hydroxylation of vitamin D3, 1 alpha-hydroxyvitamin D3 and 1 alpha-hydroxydihydrotachysterol3. In each case they also showed the ability to 26(27)-hydroxylate the cholesterol-like (D3) side chain. The relative rates of 25- and 26(27)-hydroxylation of 1 alpha-hydroxyvitamin D3 approximately mimicked the ratio of products observed in HepG2 cells. Vitamin D2 and 1 alpha-hydroxyvitamin D2, both with the ergosterol-like side chain, were 24- and 26(27)-hydroxylated by CYP27. The rate of side-chain 24-, 25-, or 26(27)-hydroxylation was greater for 1 alpha-hydroxylated vitamin D analogs than for their nonhydroxylated counterparts. We conclude that CYP27 is capable of 24-, 25-, and 26(27)-hydroxylation of vitamin D analogs and that the nature of products is partially dictated by the side chain of the substrate. This work has revealed that the cytochrome P-450 CYP27 may be important in the metabolism of vitamin D analogs used as drugs."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.org/dc/terms/identifier"doi:10.1073/pnas.90.18.8668"xsd:string
http://purl.uniprot.org/citations/7690968http://purl.org/dc/terms/identifier"doi:10.1073/pnas.90.18.8668"xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/author"Guo Y.-D."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/author"Guo Y.-D."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/author"Jones G."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/author"Jones G."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/author"Back D.W."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/author"Back D.W."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/author"Strugnell S."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/author"Strugnell S."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/pages"8668-8672"xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/pages"8668-8672"xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/title"Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/title"Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions."xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/volume"90"xsd:string
http://purl.uniprot.org/citations/7690968http://purl.uniprot.org/core/volume"90"xsd:string
http://purl.uniprot.org/citations/7690968http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7690968
http://purl.uniprot.org/citations/7690968http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7690968