Home | My Profile | Contact Us
Research Trends Products  |   order gateway  |   author gateway  |   editor gateway  
ID:
Password:
Register | Forgot Password

Author Resources
 Author Gateway
 Article submission guidelines

Editor Resources
 Editor/Referee Gateway

Agents/Distributors
 Regional Subscription Agents/Distributors
 
Current Topics in Peptide & Protein Research   Volumes    Volume 5 
Abstract
The UDP-GALNAc: polypeptide N-acetylgalactosaminyltransferase family
Laurent Lemaitre, Arnold Boersma, Daniel Tetaert
Pages: 21 - 39
Number of pages: 19
Current Topics in Peptide & Protein Research
Volume 5 

Copyright © 2003 Research Trends. All rights reserved

ABSTRACT
 
Glycosylation reactions are of great biological importance to both prokaryotes and eukaryotes, and require the coordinate action of a large number of glycosyltransferases. These enzymes have high donor and acceptor substrate specificities, and are in general limited to catalysis of one unique glycosidic linkage. Emerging evidence indicates that formation of many glycosidic linkages is covered by large homologous transferase gene families, and that the existence of multiple ezyme isoforms provides a degree if redudancy, as well as higher level of regulation of the glycoforms synthesized. More precisely, the study of the initial step of the mucin-type O-glycosylation reaction is viewed here, i.e . the in vitro and in vivo specificities of the family of UDP-GalNAc: peptide N-acetylgalactosaminyltransferase isoforms (GaNTase1- T1 to GaNTase-T9) are analysed on the basis of reactivity and/or inhibitory activity on mucin peptide motifs, the structrual  features, calatytic properties, genomic organization, and genetic expression patterns of the different members of GaNTase family are also detailed. Results from substrate binding studies suggest that (ii)multiple isoforms of GaNTases are present in various issues, and in particular glycopeptide: GaNTases (gpGaNTases); (i) the catalyzed trasfer proceed via an ordered sequential mechanism to rule in favour of particular attachment site density depending on mucin-type molecules.
Buy this Article


 
search


E-Commerce
Buy this article
Buy this volume
Subscribe to this title
Shopping Cart

Quick Links
Login
Search Products
Browse in Alphabetical Order : Journals
Series/Books
Browse by Subject Classification : Journals
Series/Books

Miscellaneous
Ordering Information Ordering Information
Downloadable forms Downloadable Forms