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http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.2.2.-
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.2.-.-
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/4.-.-.-
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#comment"In general, chondroitin sulfate (CS) and dermatan sulfate (DS) chains comprise a linkage region, a chain cap and a repeat region."xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#comment"The related enzyme EC 4.2.2.21 has the same substrate specificity but removes disaccharide residues from the non-reducing ends of both polymeric chondroitin sulfates and their oligosaccharide fragments produced by EC 4.2.2.20."xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#comment"Keratan sulfate, heparan sulfate and heparin are not substrates."xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#comment"The repeat region of CS is a repeating disaccharide of glucuronic acid (GlcA) and N-acetylgalactosamine (GalNAc) [-4)GlcA(beta1-3)GalNAc(beta1-]n, which may be O-sulfated on the C-4 and/or C-6 of GalNAc and C-2 of GlcA."xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#comment"GlcA residues of CS may be epimerized to iduronic acid (IdoA) forming the repeating disaccharide [-4)IdoA(alpha1-3)GalNAc(beta1-]n of DS."xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#comment"Chondroitin sulfate, chondroitin-sulfate proteoglycan and dermatan sulfate are the best substrates but the enzyme can also act on hyaluronan at a much lower rate."xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#comment"Both the concentrations and locations of sulfate-ester substituents vary with glucosaminoglycan source."xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2000/01/rdf-schema#comment"Degrades a variety of glycosaminoglycans of the chondroitin-sulfate- and dermatan-sulfate type."xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2004/02/skos/core#prefLabel"chondroitin-sulfate-ABC endolyase"xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9083041
http://purl.uniprot.org/enzyme/4.2.2.20http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16336265
http://purl.uniprot.org/enzyme/4.2.2.20http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/4231029
http://purl.uniprot.org/enzyme/4.2.2.20http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/5647268
http://purl.uniprot.org/enzyme/4.2.2.20http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/5647269
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2004/02/skos/core#altLabel"chondroitinase"xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2004/02/skos/core#altLabel"chondroitin ABC lyase"xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2004/02/skos/core#altLabel"chondroitin sulfate ABC endolyase"xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2004/02/skos/core#altLabel"ChS ABC lyase I"xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2004/02/skos/core#altLabel"ChS ABC lyase"xsd:string
http://purl.uniprot.org/enzyme/4.2.2.20http://www.w3.org/2004/02/skos/core#altLabel"chondroitin ABC eliminase"xsd:string