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http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.11.1.-
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.11.-.-
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2000/01/rdf-schema#comment"They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II)."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2000/01/rdf-schema#comment"Bacterial TfuDyP catalyzes sulfoxidation."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2000/01/rdf-schema#comment"The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2000/01/rdf-schema#comment"Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2004/02/skos/core#prefLabel"dye decolorizing peroxidase"xsd:string
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19967355
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19756587
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17654547
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10049859
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15313183
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19009358
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19099183
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19801472
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/20495915
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2004/02/skos/core#altLabel"DyP-type peroxidase"xsd:string
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2004/02/skos/core#altLabel"DyP"xsd:string
http://purl.uniprot.org/enzyme/1.11.1.19http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.11.1.19#SIPFA509FC8BA69B7DB
http://purl.uniprot.org/enzyme/1.11.1.19http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/1.11.1.-
http://purl.uniprot.org/uniprot/A0A023H3C9http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.11.1.19
http://purl.uniprot.org/uniprot/A0A023H2M9http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.11.1.19