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http://purl.uniprot.org/citations/17021237http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17021237http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17021237http://www.w3.org/2000/01/rdf-schema#comment"Synthetic peptides corresponding to portions of group B streptococcal peptidoglycan were used to show that the endopeptidase activity of bacteriophage B30 lysin cleaves between D-Ala in the stem peptide and L-Ala in the cross bridge and that the minimal peptide sequence cleaved is DL-gamma-Glu-Lys-D-Ala-Ala-Ala. The only glycosidase activity present is that of N-acetyl-beta-D-muramidase."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.org/dc/terms/identifier"doi:10.1128/aem.00829-06"xsd:string
http://purl.uniprot.org/citations/17021237http://purl.org/dc/terms/identifier"doi:10.1128/aem.00829-06"xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/author"Baker J.R."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/author"Baker J.R."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/author"Liu C."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/author"Liu C."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/author"Dong S."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/author"Dong S."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/author"Pritchard D.G."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/author"Pritchard D.G."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/name"Appl. Environ. Microbiol."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/name"Appl. Environ. Microbiol."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/pages"6825-6828"xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/pages"6825-6828"xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/title"Endopeptidase and glycosidase activities of the bacteriophage B30 lysin."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/title"Endopeptidase and glycosidase activities of the bacteriophage B30 lysin."xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/volume"72"xsd:string
http://purl.uniprot.org/citations/17021237http://purl.uniprot.org/core/volume"72"xsd:string
http://purl.uniprot.org/citations/17021237http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17021237
http://purl.uniprot.org/citations/17021237http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17021237