A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates

被引：110

作者：

Bennett, EP

Hassan, H

Hollingsworth, MA

Clausen, H

机构：

[1] Fac Hlth Sci, Sch Dent, DK-2200 Copenhagen N, Denmark

[2] Univ Nebraska, Med Ctr, Eppley Inst Res Canc & Allied Dis, Omaha, NE 68198 USA

来源：

FEBS LETTERS | 1999年 / 460卷 / 02期

关键词：

O-glycosylation; GalNAc-transferase; glycosyltransferase; mucin;

D O I：

10.1016/S0014-5793(99)01268-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A 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 shelved 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. (C) 1999 Federation of European Biochemical Societies.

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页码：226 / 230

页数：5

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