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http://purl.uniprot.org/citations/16593451http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16593451http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16593451http://www.w3.org/2000/01/rdf-schema#comment"An extracellular lignin-degrading enzyme from the basidiomycete Phanerochaete chrysosporium Burdsall was purified to homogeneity by ion-exchange chromatography. The 42,000-dalton ligninase contains one protoheme IX per molecule. It catalyzes, nonstereospecifically, several oxidations in the alkyl side chains of lignin-related compounds: C(alpha)-C(beta) cleavage in lignin-related compounds of the type aryl-C(alpha)HOH-C(beta)HR-C(gamma)H(2)OH (R = -aryl or -O-aryl), oxidation of benzyl alcohols to aldehydes or ketones, intradiol cleavage in phenylglycol structures, and hydroxylation of benzylic methylene groups. It also catalyzes oxidative coupling of phenols, perhaps explaining the long-recognized association between phenol oxidation and lignin degradation. All reactions require H(2)O(2). The C(alpha)-C(beta) cleavage and methylene hydroxylation reactions involve substrate oxygenation; the oxygen atom is from O(2) and not H(2)O(2). Thus the enzyme is an oxygenase, unique in its requirement for H(2)O(2)."xsd:string
http://purl.uniprot.org/citations/16593451http://purl.org/dc/terms/identifier"doi:10.1073/pnas.81.8.2280"xsd:string
http://purl.uniprot.org/citations/16593451http://purl.org/dc/terms/identifier"doi:10.1073/pnas.81.8.2280"xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/author"Kirk T.K."xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/author"Kirk T.K."xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/author"Tien M."xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/author"Tien M."xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/pages"2280-2284"xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/pages"2280-2284"xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/title"Lignin-degrading enzyme from Phanerochaete chrysosporium: purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase."xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/title"Lignin-degrading enzyme from Phanerochaete chrysosporium: purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase."xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/16593451http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/16593451http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16593451
http://purl.uniprot.org/citations/16593451http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16593451
http://purl.uniprot.org/citations/16593451http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16593451
http://purl.uniprot.org/citations/16593451http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16593451
http://purl.uniprot.org/uniprot/P06181http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16593451
http://purl.uniprot.org/uniprot/P06181#attribution-43215B6E2875842608A010086673AD2Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16593451