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http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.13.-
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.-.-
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2000/01/rdf-schema#comment"The enzyme consists of linked oxygenase and reductase domains."xsd:string
http://purl.uniprot.org/enzyme/1.14.13.39http://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/1.14.13.39http://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/1.14.13.39http://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/1.14.13.39http://www.w3.org/2004/02/skos/core#prefLabel"nitric-oxide synthase (NADPH)"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11279231
http://purl.uniprot.org/enzyme/1.14.13.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1689048
http://purl.uniprot.org/enzyme/1.14.13.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1706713
http://purl.uniprot.org/enzyme/1.14.13.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19805284
http://purl.uniprot.org/enzyme/1.14.13.39http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/21119059
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2004/02/skos/core#altLabel"NO synthase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2004/02/skos/core#altLabel"NADPH-diaphorase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2004/02/skos/core#altLabel"endothelium-derived relaxing factor synthase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2004/02/skos/core#altLabel"nitric-oxide synthetase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2004/02/skos/core#altLabel"endothelium-derived relaxation factor-forming enzyme"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.39http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.14.13.39#SIP532FF7196D5C25E9
http://purl.uniprot.org/enzyme/1.14.13.39http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/1.14.13.-
http://purl.uniprot.org/uniprot/A0A811YBU4http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.14.13.39
http://purl.uniprot.org/uniprot/A0A9W2Y143http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.14.13.39
http://purl.uniprot.org/uniprot/A0A9W9ZTI8http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.14.13.39