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http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.14.-
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.-.-
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2000/01/rdf-schema#comment"Catalyzes two independent reactions at the same active site - the 17alpha-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis, and the conversion of the 17alpha-hydroxylated products via a 17,20-lyase reaction to form androstenedione and dehydroepiandrosterone, leading to sex hormone biosynthesis (EC 1.14.14.32)."xsd:string
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2000/01/rdf-schema#comment"Requires NADPH and EC 1.6.2.4."xsd:string
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2000/01/rdf-schema#comment"The ratio of the 17alpha-hydroxylase and 17,20-lyase activities is an important factor in determining the directions of steroid hormone biosynthesis toward biosynthesis of glucocorticoid or sex hormones."xsd:string
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2004/02/skos/core#prefLabel"steroid 17alpha-monooxygenase"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12693981
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/13549484
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17386955
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18707589
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6966286
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2004/02/skos/core#altLabel"CYP17A1"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2004/02/skos/core#altLabel"CYP17"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2004/02/skos/core#altLabel"cytochrome p450 XVIIA1"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2004/02/skos/core#altLabel"steroid 17alpha-hydroxylase"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.19http://www.w3.org/2004/02/skos/core#altLabel"steroid 17alpha-hydroxylase/17,20 lyase"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/1.14.99.9
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/1.14.1.7
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/1.99.1.9
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.14.14.19#SIPC1016A1B97C83EF1
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.14.14.19#SIPA30656FAD3E87B47
http://purl.uniprot.org/enzyme/1.14.14.19http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.14.14.19#SIPA33E1FD67321FCDD