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http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.15.-
http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.-.-
http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.15.17http://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/1.14.15.17http://www.w3.org/2000/01/rdf-schema#comment"Pheophorbide b acts as an inhibitor."xsd:string
http://purl.uniprot.org/enzyme/1.14.15.17http://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/1.14.15.17http://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/1.14.15.17http://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/1.14.15.17http://www.w3.org/2004/02/skos/core#prefLabel"pheophorbide a oxygenase"xsd:string
http://purl.uniprot.org/enzyme/1.14.15.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/14657372
http://purl.uniprot.org/enzyme/1.14.15.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17237353
http://purl.uniprot.org/enzyme/1.14.15.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16844830
http://purl.uniprot.org/enzyme/1.14.15.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12223835
http://purl.uniprot.org/enzyme/1.14.15.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16669755
http://purl.uniprot.org/enzyme/1.14.15.17http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9624113
http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/2004/02/skos/core#altLabel"PAO"xsd:string
http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/2004/02/skos/core#altLabel"PaO"xsd:string
http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/2004/02/skos/core#altLabel"pheide a monooxygenase"xsd:string
http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/2004/02/skos/core#altLabel"pheide a oxygenase"xsd:string
http://purl.uniprot.org/enzyme/1.14.15.17http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/1.14.12.20
http://purl.uniprot.org/enzyme/1.14.15.17http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.14.15.17#SIP4307070F3E65EEF0
http://purl.uniprot.org/enzyme/1.14.15.17http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/1.14.15.-
http://purl.uniprot.org/uniprot/A0A251SFV0http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.14.15.17