http://purl.uniprot.org/enzyme/4.8.1.4 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.-.-.- |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.8.-.- |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/4.8.1.- |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://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/4.8.1.4 | http://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/4.8.1.4 | http://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/4.8.1.4 | http://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/4.8.1.4 | http://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/4.8.1.4 | http://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/4.8.1.4 | http://www.w3.org/2004/02/skos/core#prefLabel | "phenylacetaldoxime dehydratase"xsd:string |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/10651646 |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15596434 |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "(Z)-phenylacetaldehyde-oxime hydro-lyase"xsd:string |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "PAOx dehydratase"xsd:string |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://www.w3.org/2004/02/skos/core#altLabel | "arylacetaldoxime dehydratase"xsd:string |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://purl.uniprot.org/core/replaces | http://purl.uniprot.org/enzyme/4.99.1.7 |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/4.8.1.4#SIP01AA3E872159B483 |
http://purl.uniprot.org/enzyme/4.8.1.4 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/4.8.1.- |
http://purl.uniprot.org/uniprot/P82604 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/4.8.1.4 |
http://purl.uniprot.org/uniprot/P82604#SIP5D80EB2D2F404ADD | http://purl.uniprot.org/core/enzymeClass | http://purl.uniprot.org/enzyme/4.8.1.4 |
http://purl.uniprot.org/uniprot/#_kb.P82604_up.enzyme_E36E50C184DD1736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/enzyme/4.8.1.4 |
http://purl.uniprot.org/enzyme/4.99.1.7 | http://purl.uniprot.org/core/replacedBy | http://purl.uniprot.org/enzyme/4.8.1.4 |
http://purl.uniprot.org/enzyme/4.8.1.- | http://www.w3.org/2004/02/skos/core#narrowerTransitive | http://purl.uniprot.org/enzyme/4.8.1.4 |