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http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.13.-
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.-.-
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2000/01/rdf-schema#comment"A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines."xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2000/01/rdf-schema#comment"Generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites."xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2000/01/rdf-schema#comment"For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)."xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2000/01/rdf-schema#comment"Is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate."xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#prefLabel"flavin-containing monooxygenase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16402899
http://purl.uniprot.org/enzyme/1.14.13.8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3262153
http://purl.uniprot.org/enzyme/1.14.13.8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3949735
http://purl.uniprot.org/enzyme/1.14.13.8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/4381353
http://purl.uniprot.org/enzyme/1.14.13.8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7672012
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"FMO"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"N,N-dimethylaniline monooxygenase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"FAD-containing monooxygenase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"flavin monooxygenase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"dimethylaniline monooxygenase (N-oxide-forming)"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"DMA oxidase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"Ziegler's enzyme"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"dimethylaniline N-oxidase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"dimethylaniline oxidase"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.8http://www.w3.org/2004/02/skos/core#altLabel"flavin mixed function oxidase"xsd:string