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http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.14.-
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.-.-
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2000/01/rdf-schema#comment"The activity of this reaction is dependent on the allosteric interaction of the enzyme with cytochrome b5 without any transfer of electrons from the cytochrome."xsd:string
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2000/01/rdf-schema#comment"A microsomal protein that catalyzes two independent reactions at the same active site - the 17-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis (EC 1.14.14.19), and the conversion of the 17-hydroxylated products via a 17,20-lyase reaction to form androstenedione and 3beta-hydroxyandrost-5-en-17-one, leading to sex hormone biosynthesis."xsd:string
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2000/01/rdf-schema#comment"The enzymes from different organisms differ in their substrate specificity; while the enzymes from pig, hamster, and rat accept both 17alpha-hydroxyprogesterone and 17alpha-hydroxypregnenolone, the enzymes from human, bovine, sheep, goat, and bison do not accept the former, and the enzyme from guinea pig does not accept the latter."xsd:string
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2004/02/skos/core#prefLabel"17alpha-hydroxyprogesterone deacetylase"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.32http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9452426
http://purl.uniprot.org/enzyme/1.14.14.32http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12693981
http://purl.uniprot.org/enzyme/1.14.14.32http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/26587646
http://purl.uniprot.org/enzyme/1.14.14.32http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/26668369
http://purl.uniprot.org/enzyme/1.14.14.32http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/26976652
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2004/02/skos/core#altLabel"CYP17A1"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2004/02/skos/core#altLabel"CYP17"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2004/02/skos/core#altLabel"17alpha-hydroxyprogesterone 17,20-lyase"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2004/02/skos/core#altLabel"17alpha-hydroxyprogesterone acetaldehyde-lyase"xsd:string
http://purl.uniprot.org/enzyme/1.14.14.32http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/4.1.2.30
http://purl.uniprot.org/enzyme/1.14.14.32http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.14.14.32#SIPA30656FAD3E87B47
http://purl.uniprot.org/enzyme/1.14.14.32http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.14.14.32#SIPA6A6F2E25117E984
http://purl.uniprot.org/enzyme/1.14.14.32http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/1.14.14.-
http://purl.uniprot.org/uniprot/A0AA47M110http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.14.14.32
http://purl.uniprot.org/uniprot/A0A852CB43http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.14.14.32
http://purl.uniprot.org/uniprot/A0A091LZU8http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.14.14.32