PubMed:3242801 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":456,"end":463},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Preparation of branched hexasaccharides by the action of a viral lyase on Klebsiella K14 polysaccharide.\nKlebsiella K14 capsular polysaccharide was degraded by a bacteriophage-borne enzyme to afford oligosaccharides A-C which were studied by one- and two-dimensional n.m.r. spectroscopy. A and B were the repeating-unit hexasaccharide and pyruvylated hexasaccharide, respectively, while C was a dodecasaccharide. Each oligomer was terminated by a reducing mannose and a non-reducing 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid residue, indicating that the phage enzyme had cleaved the beta-D-Manp-(1----4)-beta-D-GlcpA linkages in the polysaccharide by a lyase, rather than the more common glycosidase, activity found with other Klebsiella bacteriophages. In this respect, the depolymerisation resembles those reported for the capsular polysaccharides of Klebsiella K5 and K64"}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":104},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":105,"end":287},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":288,"end":412},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":413,"end":763},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":764,"end":884},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":104},"obj":"Sentence"},{"id":"T2","span":{"begin":105,"end":287},"obj":"Sentence"},{"id":"T3","span":{"begin":288,"end":412},"obj":"Sentence"},{"id":"T4","span":{"begin":413,"end":763},"obj":"Sentence"},{"id":"T5","span":{"begin":764,"end":884},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Preparation of branched hexasaccharides by the action of a viral lyase on Klebsiella K14 polysaccharide.\nKlebsiella K14 capsular polysaccharide was degraded by a bacteriophage-borne enzyme to afford oligosaccharides A-C which were studied by one- and two-dimensional n.m.r. spectroscopy. A and B were the repeating-unit hexasaccharide and pyruvylated hexasaccharide, respectively, while C was a dodecasaccharide. Each oligomer was terminated by a reducing mannose and a non-reducing 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid residue, indicating that the phage enzyme had cleaved the beta-D-Manp-(1----4)-beta-D-GlcpA linkages in the polysaccharide by a lyase, rather than the more common glycosidase, activity found with other Klebsiella bacteriophages. In this respect, the depolymerisation resembles those reported for the capsular polysaccharides of Klebsiella K5 and K64"}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":456,"end":463},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Preparation of branched hexasaccharides by the action of a viral lyase on Klebsiella K14 polysaccharide.\nKlebsiella K14 capsular polysaccharide was degraded by a bacteriophage-borne enzyme to afford oligosaccharides A-C which were studied by one- and two-dimensional n.m.r. spectroscopy. A and B were the repeating-unit hexasaccharide and pyruvylated hexasaccharide, respectively, while C was a dodecasaccharide. Each oligomer was terminated by a reducing mannose and a non-reducing 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid residue, indicating that the phage enzyme had cleaved the beta-D-Manp-(1----4)-beta-D-GlcpA linkages in the polysaccharide by a lyase, rather than the more common glycosidase, activity found with other Klebsiella bacteriophages. In this respect, the depolymerisation resembles those reported for the capsular polysaccharides of Klebsiella K5 and K64"}

{"project":"GlyCosmos6-CLO","denotations":[{"id":"T1","span":{"begin":711,"end":719},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"}],"text":"Preparation of branched hexasaccharides by the action of a viral lyase on Klebsiella K14 polysaccharide.\nKlebsiella K14 capsular polysaccharide was degraded by a bacteriophage-borne enzyme to afford oligosaccharides A-C which were studied by one- and two-dimensional n.m.r. spectroscopy. A and B were the repeating-unit hexasaccharide and pyruvylated hexasaccharide, respectively, while C was a dodecasaccharide. Each oligomer was terminated by a reducing mannose and a non-reducing 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid residue, indicating that the phage enzyme had cleaved the beta-D-Manp-(1----4)-beta-D-GlcpA linkages in the polysaccharide by a lyase, rather than the more common glycosidase, activity found with other Klebsiella bacteriophages. In this respect, the depolymerisation resembles those reported for the capsular polysaccharides of Klebsiella K5 and K64"}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":74,"end":84},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":105,"end":115},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":162,"end":175},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":737,"end":747},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":748,"end":762},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":863,"end":873},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"NCBItxid:570"},{"id":"A2","pred":"db_id","subj":"T2","obj":"NCBItxid:570"},{"id":"A3","pred":"db_id","subj":"T3","obj":"NCBItxid:38018"},{"id":"A4","pred":"db_id","subj":"T4","obj":"NCBItxid:570"},{"id":"A5","pred":"db_id","subj":"T5","obj":"NCBItxid:38018"},{"id":"A6","pred":"db_id","subj":"T6","obj":"NCBItxid:570"}],"text":"Preparation of branched hexasaccharides by the action of a viral lyase on Klebsiella K14 polysaccharide.\nKlebsiella K14 capsular polysaccharide was degraded by a bacteriophage-borne enzyme to afford oligosaccharides A-C which were studied by one- and two-dimensional n.m.r. spectroscopy. A and B were the repeating-unit hexasaccharide and pyruvylated hexasaccharide, respectively, while C was a dodecasaccharide. Each oligomer was terminated by a reducing mannose and a non-reducing 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid residue, indicating that the phage enzyme had cleaved the beta-D-Manp-(1----4)-beta-D-GlcpA linkages in the polysaccharide by a lyase, rather than the more common glycosidase, activity found with other Klebsiella bacteriophages. In this respect, the depolymerisation resembles those reported for the capsular polysaccharides of Klebsiella K5 and K64"}