http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.14.99.- |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.14.-.- |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2000/01/rdf-schema#comment | "During the reaction the substrate is oxidized by the FAD cofactor of the enzyme to generate the corresponding imine, which is subsequently hydrolyzed in the form of formaldehyde."xsd:string |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2000/01/rdf-schema#comment | "The physiological electron acceptor is not known with certainty. In vitro the enzyme can use oxygen, which is reduced to hydrogen peroxide, but generation of hydrogen peroxide in the chromatin environment is unlikely as it will result in oxidative damage of DNA."xsd:string |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme is similar to flavin amine oxidases, and differs from all other known histone lysine demethylases, which are iron(II)- and 2-oxoglutarate-dependent dioxygenases."xsd:string |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme specifically removes methyl groups from mono- and dimethylated lysine(4) of histone 3."xsd:string |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2004/02/skos/core#prefLabel | "[histone-H3]-N(6),N(6)-dimethyl-L-lysine(4) FAD-dependent demethylase"xsd:string |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15811342 |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/19624733 |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2004/02/skos/core#altLabel | "lysine-specific histone demethylase 1"xsd:string |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.14.99.66#SIP6A02D6CFD333672F |
http://purl.uniprot.org/enzyme/1.14.99.66 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.14.99.- |
http://purl.uniprot.org/uniprot/A0A8D3EAW3 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |
http://purl.uniprot.org/uniprot/A0A9J8CYA6 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |
http://purl.uniprot.org/uniprot/B7Z0G7 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |
http://purl.uniprot.org/uniprot/Q8NB78 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |
http://purl.uniprot.org/uniprot/A0A4W4EY94 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |
http://purl.uniprot.org/uniprot/A0A6A5EFF6 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |
http://purl.uniprot.org/uniprot/A0A667H3X0 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |
http://purl.uniprot.org/uniprot/A0A6J1ZF10 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |
http://purl.uniprot.org/uniprot/A0A6P6IND5 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |
http://purl.uniprot.org/uniprot/A0A811YLW0 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.14.99.66 |