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http://purl.uniprot.org/citations/8280099http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8280099http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8280099http://www.w3.org/2000/01/rdf-schema#comment"Tetrahymena pyriformis was found to exhibit high NADPH-dependent 20-oxosteroid reductase activity that converted 17 alpha-hydroxyprogesterone into 17 alpha,20 alpha-dihydroxypregn-4-en-3-one. The enzyme was purified 400-fold from the cytosolic fraction. The purified enzyme with a specific activity of 6.4 mumol/min per mg of protein had an isoelectric point of 4.9 and M(r) of 68,000, and was composed of two subunits of equal size. The N-terminal sequence was determined to be LAKTVPLNDGTNFPIFGG. The enzyme reduced pregnanes and pregnanes possessing a 17 alpha-hydroxy group to a greater extent than those without the hydroxy group, and oxidized 20 alpha-hydroxy groups of the steroids in the presence of NADP+. The Km values for 17 alpha-hydroxyprogesterone and 17 alpha-hydroxypregnenolone were 2.9 and 3.4 microM respectively. Although the enzyme was inactive towards androgens and oestrogens with 3- or 17-oxo groups, it reduced several nonsteroidal carbonyl compounds and oxidized trans-benzene dihydrodiol. The enzyme activity was inhibited by synthetic oestrogens, barbiturates, aldose reductase inhibitors and quercitrin. Thus, this enzyme is a novel form of 20 alpha-hydroxysteroid dehydrogenase (EC 1.1.1.149) which structurally and functionally differs from the mammalian and bacterial enzymes."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.org/dc/terms/identifier"doi:10.1042/bj2970195"xsd:string
http://purl.uniprot.org/citations/8280099http://purl.org/dc/terms/identifier"doi:10.1042/bj2970195"xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Sato K."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Sato K."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Nozawa Y."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Nozawa Y."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Hara A."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Hara A."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Inazu A."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Inazu A."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Nakayama Y."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/author"Nakayama Y."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/pages"195-200"xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/pages"195-200"xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/title"Purification and characterization of a novel dimeric 20 alpha-hydroxysteroid dehydrogenase from Tetrahymena pyriformis."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/title"Purification and characterization of a novel dimeric 20 alpha-hydroxysteroid dehydrogenase from Tetrahymena pyriformis."xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/volume"297"xsd:string
http://purl.uniprot.org/citations/8280099http://purl.uniprot.org/core/volume"297"xsd:string