http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.14.13.- |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.14.-.- |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme consists of linked oxygenase and reductase domains."xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2000/01/rdf-schema#comment | "The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin, and its two domains are linked via a regulatory calmodulin-binding domain."xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2000/01/rdf-schema#comment | "The reductase domain of the enzyme from the bacterium Sorangium cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from NADPH to the active center. cf. EC 1.14.14.47."xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2000/01/rdf-schema#comment | "Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center."xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2004/02/skos/core#prefLabel | "nitric-oxide synthase (NADPH)"xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11279231 |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1689048 |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/1706713 |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19805284 |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/21119059 |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2004/02/skos/core#altLabel | "NO synthase"xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2004/02/skos/core#altLabel | "NADPH-diaphorase"xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2004/02/skos/core#altLabel | "endothelium-derived relaxing factor synthase"xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2004/02/skos/core#altLabel | "nitric-oxide synthetase"xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2004/02/skos/core#altLabel | "endothelium-derived relaxation factor-forming enzyme"xsd:string |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.14.13.39#SIP532FF7196D5C25E9 |
http://purl.uniprot.org/enzyme/1.14.13.39 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.14.13.- |
http://purl.uniprot.org/uniprot/A0A811YBU4 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.13.39 |
http://purl.uniprot.org/uniprot/A0A9W2Y143 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.13.39 |
http://purl.uniprot.org/uniprot/A0A9W9ZTI8 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.13.39 |