http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.13.11.- |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.13.-.- |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2000/01/rdf-schema#comment | "The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyze two separate reactions."xsd:string |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2000/01/rdf-schema#comment | "The bifunctional enzyme from Gaeumannomyces graminis also catalyzes the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6)."xsd:string |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2000/01/rdf-schema#comment | "Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5)."xsd:string |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2004/02/skos/core#prefLabel | "linoleate 8R-lipoxygenase"xsd:string |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8662736 |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19286665 |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18586008 |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8117115 |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2004/02/skos/core#altLabel | "5,8-linoleate diol synthase (bifunctional enzyme)"xsd:string |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2004/02/skos/core#altLabel | "7,8-linoleate diol synthase (bifunctional enzyme)"xsd:string |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/1.13.11.44 |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.13.11.60#SIP639AD988565D47B1 |
http://purl.uniprot.org/enzyme/1.13.11.60 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.13.11.- |
http://purl.uniprot.org/uniprot/A0A9N9ZDY4 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.13.11.60 |
http://purl.uniprot.org/uniprot/A0A0H1BUH2 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.13.11.60 |
http://purl.uniprot.org/uniprot/A0A9P8UV73 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.13.11.60 |
http://purl.uniprot.org/uniprot/A0A9P9GRL5 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.13.11.60 |
http://purl.uniprot.org/uniprot/A0A9W8RPJ5 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.13.11.60 |
http://purl.uniprot.org/uniprot/A0A4Z1IV57 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.13.11.60 |
http://purl.uniprot.org/uniprot/K3VUX9 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.13.11.60 |