http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.14.15.- |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.14.-.- |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2000/01/rdf-schema#comment | "While still attached to this enzyme, the product is rapidly converted into primary fluorescent chlorophyll catabolite by the action of EC 1.3.7.12."xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2000/01/rdf-schema#comment | "Pheophorbide b acts as an inhibitor."xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme from Arabidopsis contains a Rieske-type iron-sulfur cluster and requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I."xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2000/01/rdf-schema#comment | "In (18)O2 labeling experiments, only the aldehyde oxygen is labeled, suggesting that the other oxygen atom may originate from H2O."xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2000/01/rdf-schema#comment | "This enzyme catalyzes a key reaction in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants."xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2004/02/skos/core#prefLabel | "pheophorbide a oxygenase"xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/14657372 |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17237353 |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16844830 |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12223835 |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16669755 |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9624113 |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2004/02/skos/core#altLabel | "PAO"xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2004/02/skos/core#altLabel | "PaO"xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2004/02/skos/core#altLabel | "pheide a monooxygenase"xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2004/02/skos/core#altLabel | "pheide a oxygenase"xsd:string |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/1.14.12.20 |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.14.15.17#SIP4307070F3E65EEF0 |
http://purl.uniprot.org/enzyme/1.14.15.17 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.14.15.- |
http://purl.uniprot.org/uniprot/A0A251SFV0 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.15.17 |