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http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.8.3.-
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.8.-.-
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2000/01/rdf-schema#comment"The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro."xsd:string
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2000/01/rdf-schema#comment"The enzyme, which is found in both prokaryotes and eukaryotes, catalyzes a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity."xsd:string
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2000/01/rdf-schema#comment"Glutathione alo acts in vitro, but it is not known whether it is used in vivo."xsd:string
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2004/02/skos/core#prefLabel"formylglycine-generating enzyme"xsd:string
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9748219
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16368756
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9342345
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18390551
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/25931126
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/26403223
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/27862795
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/28544744
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15657036
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2004/02/skos/core#altLabel"sulfatase-modifying factor 1"xsd:string
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2004/02/skos/core#altLabel"Calpha-formylglycine-generating enzyme 1"xsd:string
http://purl.uniprot.org/enzyme/1.8.3.7http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.8.3.7#SIPDD8F8345FCE1221B
http://purl.uniprot.org/enzyme/1.8.3.7http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/1.8.3.-
http://purl.uniprot.org/uniprot/A0AA43KTB3http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.8.3.7
http://purl.uniprot.org/uniprot/Q0P5L5http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.8.3.7
http://purl.uniprot.org/uniprot/Q1PZW3http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.8.3.7