PubMed:10336987 JSON TXT

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sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":142},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":143,"end":293},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":294,"end":403},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":404,"end":409},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":410,"end":433},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":434,"end":706},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":707,"end":974},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":975,"end":1211},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1212,"end":1372},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1373,"end":1492},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1493,"end":1656},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":142},"obj":"Sentence"},{"id":"T2","span":{"begin":143,"end":293},"obj":"Sentence"},{"id":"T3","span":{"begin":294,"end":433},"obj":"Sentence"},{"id":"T4","span":{"begin":434,"end":706},"obj":"Sentence"},{"id":"T5","span":{"begin":707,"end":974},"obj":"Sentence"},{"id":"T6","span":{"begin":975,"end":1211},"obj":"Sentence"},{"id":"T7","span":{"begin":1212,"end":1372},"obj":"Sentence"},{"id":"T8","span":{"begin":1373,"end":1492},"obj":"Sentence"},{"id":"T9","span":{"begin":1493,"end":1656},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":142},"obj":"Sentence"},{"id":"T2","span":{"begin":143,"end":293},"obj":"Sentence"},{"id":"T3","span":{"begin":294,"end":403},"obj":"Sentence"},{"id":"T4","span":{"begin":404,"end":409},"obj":"Sentence"},{"id":"T5","span":{"begin":410,"end":433},"obj":"Sentence"},{"id":"T6","span":{"begin":434,"end":706},"obj":"Sentence"},{"id":"T7","span":{"begin":707,"end":974},"obj":"Sentence"},{"id":"T8","span":{"begin":975,"end":1211},"obj":"Sentence"},{"id":"T9","span":{"begin":1212,"end":1372},"obj":"Sentence"},{"id":"T10","span":{"begin":1373,"end":1492},"obj":"Sentence"},{"id":"T11","span":{"begin":1493,"end":1656},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

GlycoBiology-PACDB

{"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":681,"end":705},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC297"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

GlycoBiology-FMA

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":50,"end":58},"obj":"FMAID:214709"},{"id":"_T2","span":{"begin":80,"end":90},"obj":"FMAID:196728"},{"id":"_T3","span":{"begin":80,"end":90},"obj":"FMAID:82739"},{"id":"_T4","span":{"begin":109,"end":123},"obj":"FMAID:61795"},{"id":"_T5","span":{"begin":109,"end":123},"obj":"FMAID:165243"},{"id":"_T6","span":{"begin":507,"end":522},"obj":"FMAID:82742"},{"id":"_T7","span":{"begin":507,"end":522},"obj":"FMAID:196731"},{"id":"_T8","span":{"begin":537,"end":543},"obj":"FMAID:30332"},{"id":"_T9","span":{"begin":537,"end":543},"obj":"FMAID:171168"},{"id":"_T10","span":{"begin":544,"end":554},"obj":"FMAID:196728"},{"id":"_T11","span":{"begin":544,"end":554},"obj":"FMAID:82739"},{"id":"_T12","span":{"begin":574,"end":583},"obj":"FMAID:196741"},{"id":"_T13","span":{"begin":574,"end":583},"obj":"FMAID:82752"},{"id":"_T14","span":{"begin":633,"end":637},"obj":"FMAID:198663"},{"id":"_T15","span":{"begin":709,"end":721},"obj":"FMAID:82784"},{"id":"_T16","span":{"begin":709,"end":721},"obj":"FMAID:196778"},{"id":"_T17","span":{"begin":924,"end":936},"obj":"FMAID:82737"},{"id":"_T18","span":{"begin":924,"end":936},"obj":"FMAID:197276"},{"id":"_T19","span":{"begin":1031,"end":1043},"obj":"FMAID:197276"},{"id":"_T20","span":{"begin":1031,"end":1043},"obj":"FMAID:82737"},{"id":"_T21","span":{"begin":1186,"end":1201},"obj":"FMAID:196731"},{"id":"_T22","span":{"begin":1186,"end":1201},"obj":"FMAID:82742"},{"id":"_T23","span":{"begin":1344,"end":1350},"obj":"FMAID:30332"},{"id":"_T24","span":{"begin":1344,"end":1350},"obj":"FMAID:171168"},{"id":"_T25","span":{"begin":1630,"end":1645},"obj":"FMAID:82742"},{"id":"_T26","span":{"begin":1630,"end":1645},"obj":"FMAID:196731"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":1015,"end":1018},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T2","span":{"begin":1019,"end":1022},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T3","span":{"begin":1144,"end":1147},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T4","span":{"begin":1170,"end":1173},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T5","span":{"begin":1278,"end":1281},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T6","span":{"begin":1282,"end":1285},"obj":"http://www.uniprot.org/uniprot/Q61024"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":681,"end":694},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4895"},{"id":"T2","span":{"begin":681,"end":694},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4930"},{"id":"T3","span":{"begin":681,"end":694},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/36034"},{"id":"T4","span":{"begin":681,"end":694},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4891"},{"id":"T5","span":{"begin":1379,"end":1387},"obj":"http://purl.bioontology.org/ontology/STY/T033"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":0,"end":13},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T2","span":{"begin":197,"end":209},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T3","span":{"begin":269,"end":281},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T4","span":{"begin":455,"end":468},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T5","span":{"begin":1453,"end":1466},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T6","span":{"begin":387,"end":389},"obj":"http://purl.obolibrary.org/obo/GO_0004306"},{"id":"T7","span":{"begin":783,"end":789},"obj":"http://purl.obolibrary.org/obo/GO_0007586"},{"id":"T8","span":{"begin":842,"end":853},"obj":"http://purl.obolibrary.org/obo/GO_0009056"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":980,"end":983},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T2","span":{"begin":1023,"end":1026},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T3","span":{"begin":1176,"end":1179},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T4","span":{"begin":1286,"end":1289},"obj":"http://purl.obolibrary.org/obo/GO_0005790"},{"id":"T5","span":{"begin":1290,"end":1293},"obj":"http://purl.obolibrary.org/obo/GO_0005790"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":44,"end":49},"obj":"http://edamontology.org/topic_0782"},{"id":"T2","span":{"begin":44,"end":49},"obj":"http://edamontology.org/topic_2817"},{"id":"T3","span":{"begin":80,"end":90},"obj":"http://edamontology.org/topic_0154"},{"id":"T4","span":{"begin":143,"end":148},"obj":"http://edamontology.org/topic_0782"},{"id":"T5","span":{"begin":143,"end":148},"obj":"http://edamontology.org/topic_2817"},{"id":"T6","span":{"begin":334,"end":342},"obj":"http://edamontology.org/topic_3168"},{"id":"T7","span":{"begin":334,"end":342},"obj":"http://edamontology.org/topic_0080"},{"id":"T8","span":{"begin":544,"end":554},"obj":"http://edamontology.org/topic_0154"},{"id":"T9","span":{"begin":823,"end":832},"obj":"http://edamontology.org/topic_0080"},{"id":"T10","span":{"begin":823,"end":832},"obj":"http://edamontology.org/topic_3168"},{"id":"T11","span":{"begin":924,"end":936},"obj":"http://edamontology.org/topic_0152"},{"id":"T12","span":{"begin":1031,"end":1043},"obj":"http://edamontology.org/topic_0152"},{"id":"T13","span":{"begin":1120,"end":1127},"obj":"http://edamontology.org/topic_3678"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":334,"end":342},"obj":"http://edamontology.org/operation_3218"},{"id":"T2","span":{"begin":334,"end":342},"obj":"http://edamontology.org/data_2044"},{"id":"T3","span":{"begin":544,"end":558},"obj":"http://edamontology.org/data_2016"},{"id":"T4","span":{"begin":584,"end":591},"obj":"http://edamontology.org/data_1756"},{"id":"T5","span":{"begin":823,"end":832},"obj":"http://edamontology.org/data_2044"},{"id":"T6","span":{"begin":823,"end":832},"obj":"http://edamontology.org/operation_3218"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":537,"end":543},"obj":"http://purl.obolibrary.org/obo/MAT_0000488"},{"id":"T2","span":{"begin":1344,"end":1350},"obj":"http://purl.obolibrary.org/obo/MAT_0000488"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

Lectin

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":390,"end":392},"obj":"https://acgg.asia/db/lfdb/LfDB0344"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}

GlyTouCan-IUPAC

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":681,"end":705},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"4932"}],"text":"Glycosylation of the overlapping sequons in yeast external invertase: effect of amino acid variation on site selectivity in vivo and in vitro.\nYeast invertase contains 14 sequons, all of which are glycosylated to varying degrees except for sequon 5 which is marginally glycosylated, if at all. This sequon overlaps with sequon 4 in a sequence consisting of Asn92-Asn93-Thr94-Ser95(Reddy et al., 1988, J. Biol. Chem., 263, 6978-6985). To determine whether glycosylation at Asn93is sterically hindered by the oligosaccharide on Asn92, the latter amino acid was converted to a glutamine residue by site-directed mutagenesis of the SUC2 gene in a plasmid vector which was expressed in Saccharomyces cerevisiae. A glycopeptide encompassing sequons 3 through 6 was purified from a tryptic digest of the mutagenized invertase and sequenced by Edman degradation, which revealed that Asn93 of sequon 5 contained very little, if any, carbohydrate, despite the elimination of sequon 4. When Ser and Thr were inverted to yield Asn-Asn-Ser-Thr carbohydrate was associated primarily with the second sequon, in agreement with numerous studies indicating that Asn-X-Thr is preferred to Asn-X-Ser as an oligosaccharide acceptor. However, when the invertase overlapping sequons were converted to Asn-Asn-Ser-Ser, both sequons were clearly glycosylated, with the latter sequon predominating. These findings rule out steric hindrance as a factor involved in preventing the glycosylation of sequon 5 in invertase. Comparable results were obtained using an in vitro system with sequon-containing tri- and tetrapeptides acceptors, in addition to larger oligosaccharide acceptors."}