PubMed:19282391 / 657-1161 JSONTXT

{"project":"sentences","denotations":[{"id":"TextSentencer_T4","span":{"begin":0,"end":246},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":247,"end":504},"obj":"Sentence"},{"id":"T4","span":{"begin":0,"end":504},"obj":"Sentence"},{"id":"T4","span":{"begin":0,"end":246},"obj":"Sentence"},{"id":"T5","span":{"begin":247,"end":504},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation."}

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{"project":"GlycoBiology-FMA","denotations":[{"id":"_T17","span":{"begin":287,"end":300},"obj":"FMAID:74531"},{"id":"_T18","span":{"begin":287,"end":300},"obj":"FMAID:179268"},{"id":"_T19","span":{"begin":482,"end":489},"obj":"FMAID:67257"},{"id":"_T20","span":{"begin":482,"end":489},"obj":"FMAID:165447"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation."}

{"project":"uniprot-human","denotations":[{"id":"T2","span":{"begin":199,"end":202},"obj":"http://www.uniprot.org/uniprot/P21941"}],"text":"In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T8","span":{"begin":102,"end":122},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/197"},{"id":"T9","span":{"begin":330,"end":339},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/127244"}],"text":"In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation."}

{"project":"GO-BP","denotations":[{"id":"T2","span":{"begin":157,"end":169},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T3","span":{"begin":448,"end":460},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T6","span":{"begin":321,"end":329},"obj":"http://purl.obolibrary.org/obo/GO_0007349"},{"id":"T7","span":{"begin":482,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0006486"},{"id":"T8","span":{"begin":490,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation."}

{"project":"NCBITAXON","denotations":[{"id":"T6","span":{"begin":102,"end":122},"obj":"OrganismTaxon"}],"attributes":[{"id":"A6","pred":"db_id","subj":"T6","obj":"197"}],"text":"In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation."}