| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.17.-.- |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.17.99.- |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2000/01/rdf-schema#comment | "The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration."xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2000/01/rdf-schema#comment | "However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate and not via hydration of a 24(25) double bond."xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2000/01/rdf-schema#comment | "Requires ATP."xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2000/01/rdf-schema#comment | "In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate."xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2004/02/skos/core#prefLabel | "3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase"xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9218493 |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12543708 |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8856068 |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2156865 |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/240854 |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2004/02/skos/core#altLabel | "trihydroxycoprostanoyl-CoA oxidase"xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2004/02/skos/core#altLabel | "THCA-CoA oxidase"xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2004/02/skos/core#altLabel | "3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase"xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2004/02/skos/core#altLabel | "THC-CoA oxidase"xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2004/02/skos/core#altLabel | "3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate 24-hydroxylase"xsd:string |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.17.99.3#SIP4BC4B7A2ED86FE0D |
| http://purl.uniprot.org/enzyme/1.17.99.3 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.17.99.- |
| http://purl.uniprot.org/uniprot/A0A061II13 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.17.99.3 |
| http://purl.uniprot.org/uniprot/P97562 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.17.99.3 |
| http://purl.uniprot.org/uniprot/Q99424 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.17.99.3 |