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http://purl.uniprot.org/citations/2509201http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2509201http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2509201http://www.w3.org/2000/01/rdf-schema#comment"Pravastatin sodium (CS-514) is a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a key enzyme in cholesterol biosynthesis. This compound is obtained by microbial hydroxylation of sodium ML-236B (compactin) carboxylate. The soluble cytochrome P-450 was induced by sodium ML-236B carboxylate in Streptomyces carbophilus of Actinomycetes as detected in its cell-free extract. This cytochrome P-450 was designated as cytochrome P-450sca after its origin. Cytochrome P-450sca was purified by successive chromatography on anion-exchange, gel filtration and hydroxyapatite columns. On hydroxyapatite cytochrome P-450sca was further separated into minor and major peaks, designated cytochrome P-450sca-1 and cytochrome P-450sca-2, respectively. Each peak yielded a single band on sodium dodecyl sulfate/polyacrylamide gels with molecular masses of 46 +/-1 kDa. The activity hydroxylating sodium ML-236B carboxylate to pravastatin sodium was reconstituted in the presence of an electron transport system, an NADPH-generating system and oxygen. The Ks values of the cytochromes P-450sca-1 and P-450sca-2 for sodium ML-236B carboxylate were 179 microM and 229 microM, respectively. The CO versus reduced difference spectra of both cytochromes P-450 showed an absorption maximum at 448.5 nm. Their substrate difference spectra with sodium ML-236B carboxylate showed an absorption maximum at 386 nm. Amino acid analysis indicated that cytochrome P-450sca-1 and P-450sca-2 contained 46% and 47% hydrophobic residues, respectively. On Western blotting, cytochromes P-450sca-1 and P-450sca-2 were immunologically identical."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1989.tb15070.x"xsd:string
http://purl.uniprot.org/citations/2509201http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1989.tb15070.x"xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Nakahara K."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Nakahara K."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Hosobuchi M."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Hosobuchi M."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Matsuoka T."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Matsuoka T."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Miyakoshi S."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Miyakoshi S."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Serizawa N."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Serizawa N."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Tanzawa K."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/author"Tanzawa K."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/pages"707-713"xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/pages"707-713"xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/title"Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase."xsd:string
http://purl.uniprot.org/citations/2509201http://purl.uniprot.org/core/title"Purification and characterization of cytochrome P-450sca from Streptomyces carbophilus. ML-236B (compactin) induces a cytochrome P-450sca in Streptomyces carbophilus that hydroxylates ML-236B to pravastatin sodium (CS-514), a tissue-selective inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase."xsd:string
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