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http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.11.1.-
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.11.-.-
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"Involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"However larger lignin molecules can be degraded in the presence of veratryl alcohol."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"This form can be rescued by interaction with two molecules of the free radical products."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"The enzyme can act on a wide range of aromatic compounds, including methoxybenzenes and nonphenolic beta-O-4 linked arylglycerol beta-aryl ethers, but cannot act directly on the lignin molecule, which is too large to fit into the active site."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (Fe(IV)=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"In the presence of high concentration of hydrogen peroxide and lack of substrate, the enzyme forms a catalytically inactive form (compound III)."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (Fe(IV)=O radical cation) at the active site."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2000/01/rdf-schema#comment"It has been suggested that the free radical that is formed when the enzyme acts on veratryl alcohol can diffuse into the lignified cell wall, where it oxidizes lignin and other organic substrates."xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://www.w3.org/2004/02/skos/core#prefLabel"lignin peroxidase"xsd:string
http://purl.uniprot.org/enzyme/1.11.1.14http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2162833
http://purl.uniprot.org/enzyme/1.11.1.14http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2328240
http://purl.uniprot.org/enzyme/1.11.1.14http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/25649492
http://purl.uniprot.org/enzyme/1.11.1.14http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2982828
http://purl.uniprot.org/enzyme/1.11.1.14http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3080953
http://purl.uniprot.org/enzyme/1.11.1.14http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8527462
http://purl.uniprot.org/enzyme/1.11.1.14http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8639588
http://purl.uniprot.org/enzyme/1.11.1.14http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9369491
http://purl.uniprot.org/enzyme/1.11.1.14http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9790672