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http://purl.uniprot.org/enzyme/3.4.23.32http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/3.4.23.32http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.4.-.-
http://purl.uniprot.org/enzyme/3.4.23.32http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.4.23.-
http://purl.uniprot.org/enzyme/3.4.23.32http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/3.-.-.-
http://purl.uniprot.org/enzyme/3.4.23.32http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/3.4.23.32http://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/3.4.23.32http://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/3.4.23.32http://www.w3.org/2000/01/rdf-schema#comment"Belongs to peptidase family G1."xsd:string
http://purl.uniprot.org/enzyme/3.4.23.32http://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/3.4.23.32http://www.w3.org/2000/01/rdf-schema#comment"Isolated from the imperfect fungus Scytalidium lignicolum."xsd:string
http://purl.uniprot.org/enzyme/3.4.23.32http://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/3.4.23.32http://www.w3.org/2004/02/skos/core#prefLabel"scytalidopepsin B"xsd:string
http://purl.uniprot.org/enzyme/3.4.23.32http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6370989
http://purl.uniprot.org/enzyme/3.4.23.32http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3519605
http://purl.uniprot.org/enzyme/3.4.23.32http://www.w3.org/2004/02/skos/core#altLabel"Scytalidium aspartic proteinase B"xsd:string
http://purl.uniprot.org/enzyme/3.4.23.32http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/3.4.23.32#SIP921AC0E373224806
http://purl.uniprot.org/enzyme/3.4.23.32http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/3.4.23.-
http://purl.uniprot.org/uniprot/P15369http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/3.4.23.32
http://purl.uniprot.org/uniprot/P15369#SIP4DE179272A380910http://purl.uniprot.org/core/enzymeClasshttp://purl.uniprot.org/enzyme/3.4.23.32
http://purl.uniprot.org/enzyme/3.4.23.-http://www.w3.org/2004/02/skos/core#narrowerTransitivehttp://purl.uniprot.org/enzyme/3.4.23.32