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http://purl.uniprot.org/enzyme/2.3.1.313http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.1.313http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.-.-
http://purl.uniprot.org/enzyme/2.3.1.313http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.3.1.-
http://purl.uniprot.org/enzyme/2.3.1.313http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/2.-.-.-
http://purl.uniprot.org/enzyme/2.3.1.313http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/2.3.1.313http://www.w3.org/2000/01/rdf-schema#comment"The enzyme, a member of the sirtuin family, removes the lipoyl group from the dihydrolipoamide acyltransferase (E2) component of 2-oxo acid dehydrogenase complexes such as EC 1.2.1.104."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.313http://www.w3.org/2000/01/rdf-schema#comment"The enzyme often has additional activities and can remove other modifications of lysine residues such as acetyl and biotinyl groups. cf. EC 3.5.1.138."xsd:string
http://purl.uniprot.org/enzyme/2.3.1.313http://www.w3.org/2004/02/skos/core#prefLabel"NAD-dependent lipoamidase"xsd:string
http://purl.uniprot.org/enzyme/2.3.1.313http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/28900027
http://purl.uniprot.org/enzyme/2.3.1.313http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/25525879
http://purl.uniprot.org/enzyme/2.3.1.313http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/30913880
http://purl.uniprot.org/enzyme/2.3.1.313http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/2.3.1.313#SIP5A7BEA6A3D83E89E
http://purl.uniprot.org/enzyme/2.3.1.313http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/2.3.1.-
http://purl.uniprot.org/enzyme/2.3.1.-http://www.w3.org/2004/02/skos/core#narrowerTransitivehttp://purl.uniprot.org/enzyme/2.3.1.313