PubMed:10544240 JSONTXT

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":90,"end":99},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"T2","span":{"begin":298,"end":307},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"T3","span":{"begin":335,"end":344},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"T4","span":{"begin":534,"end":543},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"T5","span":{"begin":792,"end":801},"obj":"https://acgg.asia/db/ggdb/info/gg093"}],"text":"A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates.\nA novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation."}

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":90,"end":99},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"T2","span":{"begin":298,"end":307},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"T3","span":{"begin":335,"end":344},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"T4","span":{"begin":534,"end":543},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"T5","span":{"begin":792,"end":801},"obj":"https://acgg.asia/db/ggdb/info/gg093"}],"text":"A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates.\nA novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":90,"end":99},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":287,"end":297},"obj":"url"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":298,"end":307},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":335,"end":344},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":534,"end":543},"obj":"https://acgg.asia/db/ggdb/info/gg093"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":570,"end":575},"obj":"https://acgg.asia/db/ggdb/info/gg171"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":792,"end":801},"obj":"https://acgg.asia/db/ggdb/info/gg093"}],"text":"A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates.\nA novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation."}