4.5 Article

Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15

Journal

FEBS LETTERS
Volume 566, Issue 1-3, Pages 17-24

Publisher

WILEY
DOI: 10.1016/j.febslet.2004.03.108

Keywords

UDP-GaINAc : polypeptide; N-acetylgalactosaminyltransferase (EC 2.4.1.41); O-glycosylation; O-glycan; mucin

Ask authors/readers for more resources

We have cloned, expressed and characterized a novel member of the human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family, pp-GalNAc-T15. The pp-GalNAc-T15 transcript was ubiquitously expressed in human tissues. Recombinant pp-GalNAc-T15 transferred N-acetylgalactosamine (GalNAc) toward a panel of mucin-derived peptide substrates in vitro. Although pp-GalNAc-T15 showed significantly less catalytic activity than pp-GalNAc-T2, T15 transferred up to seven GalNAcs to the Muc5AC peptide, while T2 transferred up to five GalNAcs. These results clearly indicated that pp-GalNAc-T15 is a novel member of the human pp-GalNAc-T family with unique catalytic activity. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available