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http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.-.-.-
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.8.-.-
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.8.1.-
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#comment"In this way, the oxidation state of the heme controls the coordination stucture of the substrate--heme complex, which regulates enzyme activity."xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#comment"However, it is inactive with phenylacetaldoximes that have a substituent group at an alpha-site of an oxime group, for example, with (E/Z)-2-phenylpropionaldoxime and (E/Z)-mandelaldoxime."xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#comment"(Z)-Phenylacetaldoxime binds to ferric heme (the iron(III) form) via the oxygen atom whereas it binds to the active ferrous form via the nitrogen atom."xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#comment"The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron of which must be in the form iron(II) for activity."xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#comment"The enzyme is active toward several (Z)-arylacetaldoximes and (E/Z)-alkylaldoximes as well as toward arylalkylaldoximes such as 3-phenylpropionaldoxime and 4-phenylbutyraldoxime."xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2000/01/rdf-schema#comment"The activity of the enzyme is inhibited completely by the heavy-metal cations Cu(+), Cu(2+), Ag(+) and Hg(+) whereas Fe(2+) and Sn(2+) have an activatory effect."xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2004/02/skos/core#prefLabel"phenylacetaldoxime dehydratase"xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10651646
http://purl.uniprot.org/enzyme/4.8.1.4http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15596434
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2004/02/skos/core#altLabel"(Z)-phenylacetaldehyde-oxime hydro-lyase"xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2004/02/skos/core#altLabel"PAOx dehydratase"xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2004/02/skos/core#altLabel"arylacetaldoxime dehydratase"xsd:string
http://purl.uniprot.org/enzyme/4.8.1.4http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/4.99.1.7
http://purl.uniprot.org/enzyme/4.8.1.4http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/4.8.1.4#SIP01AA3E872159B483
http://purl.uniprot.org/enzyme/4.8.1.4http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/4.8.1.-
http://purl.uniprot.org/uniprot/P82604http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/4.8.1.4
http://purl.uniprot.org/uniprot/P82604#SIP5D80EB2D2F404ADDhttp://purl.uniprot.org/core/enzymeClasshttp://purl.uniprot.org/enzyme/4.8.1.4
http://purl.uniprot.org/uniprot/#_kb.P82604_up.enzyme_E36E50C184DD1736http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/enzyme/4.8.1.4
http://purl.uniprot.org/enzyme/4.99.1.7http://purl.uniprot.org/core/replacedByhttp://purl.uniprot.org/enzyme/4.8.1.4
http://purl.uniprot.org/enzyme/4.8.1.-http://www.w3.org/2004/02/skos/core#narrowerTransitivehttp://purl.uniprot.org/enzyme/4.8.1.4