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

FEBS Letters

Bennett, Eric Paul²  Hollingsworth, Michael A.¹  Hassan, Helle²  Clausen, Henrik² 

[1] Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, 600 S 42nd Street, Omaha, NE 68198, USA;Faculty of Health Sciences, School of Dentistry, Nørre Alle 20, DK-2200 Copenhagen N, Denmark

关键词: O-Glycosylation;    GalNAc-transferase;    Glycosyltransferase;    Mucin;    GalNAc;    N-acetylgalactosamine;    GalNAc-transferase;    UDP-GalNAc:polypeptide αGalNAc-transferase (EC 2.4.1.41);    EST;    expressed sequence tags;    RACE;    rapid amplification of cDNA ends;   

DOI  :  10.1016/S0014-5793(99)01268-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 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.

【 授权许可】

Unknown