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http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.1.-.-
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.1.6.-
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.-.-.-
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2000/01/rdf-schema#comment"Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-beta-lactamase fold and binds two zinc ions as cofactors."xsd:string
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2000/01/rdf-schema#comment"The key catalytic residue 3-oxo-L-alanine initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate."xsd:string
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2000/01/rdf-schema#comment"Arylsulfatases are type I enzymes, found in both prokaryotes and eukaryotes, with rather similar specificities."xsd:string
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2000/01/rdf-schema#comment"This residue is generated by post-translational modification of a conserved cysteine or serine residue by EC 1.8.3.7, EC 1.1.98.7, or EC 1.8.98.7."xsd:string
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2004/02/skos/core#prefLabel"arylsulfatase (type I)"xsd:string
http://purl.uniprot.org/enzyme/3.1.6.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9748219
http://purl.uniprot.org/enzyme/3.1.6.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7628016
http://purl.uniprot.org/enzyme/3.1.6.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/13363831
http://purl.uniprot.org/enzyme/3.1.6.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/13744184
http://purl.uniprot.org/enzyme/3.1.6.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/13772
http://purl.uniprot.org/enzyme/3.1.6.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/13843260
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2004/02/skos/core#altLabel"sulfatase"xsd:string
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2004/02/skos/core#altLabel"aryl-sulfate sulphohydrolase"xsd:string
http://purl.uniprot.org/enzyme/3.1.6.1http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/3.1.6.1#SIP03827CC58597E4D2
http://purl.uniprot.org/enzyme/3.1.6.1http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/3.1.6.-
http://purl.uniprot.org/uniprot/A0A0A8K341http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.1.6.1
http://purl.uniprot.org/uniprot/A0A9P8UES9http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.1.6.1
http://purl.uniprot.org/uniprot/A0A916JTX5http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.1.6.1
http://purl.uniprot.org/uniprot/Q3TYD4http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.1.6.1
http://purl.uniprot.org/uniprot/A0A173UWU6http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.1.6.1