http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.-.- |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.4.23.- |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/3.-.-.- |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#comment | "One of the smallest aspartic endopeptidases active as the monomer, with molecular weight 22 kDa."xsd:string |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#comment | "A second endopeptidase from S.lignicolum (see scytalidopepsin A) that is insensitive to pepstatin and methyl 2-diazoacetamidohexanoate."xsd:string |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#comment | "Belongs to peptidase family G1."xsd:string |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#comment | "Similarly inhibitor-resistant endopeptidases are found in the basidiomycetes Lentinus edodes and Ganoderma lucidum, and in Polyporus tulipiferae (a second endopeptidase distinct from polyporopepsin), but these are of typical aspartic endopeptidase size."xsd:string |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#comment | "Isolated from the imperfect fungus Scytalidium lignicolum."xsd:string |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2000/01/rdf-schema#comment | "1,2-epoxy-3-(p-nitrophenoxy)propane reacts with Glu-53, which replaces one of the aspartic residues at the active center."xsd:string |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2004/02/skos/core#prefLabel | "scytalidopepsin B"xsd:string |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/6370989 |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/3519605 |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2004/02/skos/core#altLabel | "Scytalidium aspartic proteinase B"xsd:string |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://purl.uniprot.org/core/activity | http://purl.uniprot.org/enzyme/3.4.23.32#SIP921AC0E373224806 |
http://purl.uniprot.org/enzyme/3.4.23.32 | http://www.w3.org/2004/02/skos/core#broaderTransitive | http://purl.uniprot.org/enzyme/3.4.23.- |
http://purl.uniprot.org/uniprot/P15369 | http://purl.uniprot.org/core/enzyme | http://purl.uniprot.org/enzyme/3.4.23.32 |
http://purl.uniprot.org/uniprot/P15369#SIP4DE179272A380910 | http://purl.uniprot.org/core/enzymeClass | http://purl.uniprot.org/enzyme/3.4.23.32 |
http://purl.uniprot.org/enzyme/3.4.23.- | http://www.w3.org/2004/02/skos/core#narrowerTransitive | http://purl.uniprot.org/enzyme/3.4.23.32 |