http://purl.uniprot.org/enzyme/1.8.3.7 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.-.-.- |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.8.3.- |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/1.8.-.- |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://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/1.8.3.7 | http://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/1.8.3.7 | http://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/1.8.3.7 | http://www.w3.org/2004/02/skos/core#prefLabel | "formylglycine-generating enzyme"xsd:string |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9748219 |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/16368756 |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9342345 |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/18390551 |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/25931126 |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/26403223 |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/27862795 |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/28544744 |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15657036 |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://www.w3.org/2004/02/skos/core#altLabel | "sulfatase-modifying factor 1"xsd:string |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://www.w3.org/2004/02/skos/core#altLabel | "Calpha-formylglycine-generating enzyme 1"xsd:string |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/1.8.3.7#SIPDD8F8345FCE1221B |
http://purl.uniprot.org/enzyme/1.8.3.7 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/1.8.3.- |
http://purl.uniprot.org/uniprot/A0AA43KTB3 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.8.3.7 |
http://purl.uniprot.org/uniprot/Q0P5L5 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.8.3.7 |
http://purl.uniprot.org/uniprot/Q1PZW3 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/1.8.3.7 |