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http://purl.uniprot.org/citations/12244070http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12244070http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12244070http://www.w3.org/2000/01/rdf-schema#comment"We report the identification, molecular cloning, and characterization of an endo-beta-N-acetylglucosaminidase from the nematode Caenorhabditis elegans. A search of the C. elegans genome database revealed the existence of a gene exhibiting 34% identity to Mucor hiemalis (a fungus) endo-beta-N-acetylglucosaminidase (Endo-M). Actually, the C. elegans extract contained endo-beta-N-acetylglucosaminidase activity. The putative cDNA for the C. elegans endo-beta-N-acetylglucosaminidase (Endo-CE) was amplified by polymerase chain reaction from the Uni-ZAP XR library, cloned, and sequenced. The recombinant Endo-CE expressed in Escherichia coli exhibited substrate specificity mainly for high-mannose type oligosaccharides. Man(8)GlcNAc(2) was the best substrate for Endo-CE, and Man(3)GlcNAc(2) was also hydrolyzed. Biantennary complex type oligosaccharides were poor substrates, and triantennary complex substrates were not hydrolyzed. Its substrate specificity was similar to those of Endo-M and endo-beta-N-acetylglucosaminidase from hen oviduct. Endo-CE was confirmed to exhibit transglycosylation activity, as seen for some microbial endo-beta-N-acetylglucosaminidases. This is the first report of the molecular cloning of an endo-beta-N-acetylglucosaminidase gene from a multicellular organism, which shows the possibility of using this well-characterized nematode as a model system for elucidating the role of this enzyme."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.org/dc/terms/identifier"doi:10.1093/glycob/cwf073"xsd:string
http://purl.uniprot.org/citations/12244070http://purl.org/dc/terms/identifier"doi:10.1093/glycob/cwf073"xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Fujita K."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Fujita K."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Kato T."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Kato T."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Takeuchi M."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Takeuchi M."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Yamamoto K."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Yamamoto K."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Kobayashi K."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Kobayashi K."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Kumagai H."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Kumagai H."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Natsuka S."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Ikura K."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Ikura K."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/author"Katsuka S."xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/name"Glycobiology"xsd:string
http://purl.uniprot.org/citations/12244070http://purl.uniprot.org/core/name"Glycobiology"xsd:string