Skip Navigation


Glycobiology Advance Access originally published online on January 29, 2009
Glycobiology 2009 19(5):509-517; doi:10.1093/glycob/cwp010
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Data
Right arrow All Versions of this Article:
19/5/509    most recent
cwp010v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Bojarová, P.
Right arrow Articles by Kren, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bojarová, P.
Right arrow Articles by Kren, V.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Synthesis of LacdiNAc-terminated glycoconjugates by mutant galactosyltransferase – A way to new glycodrugs and materials

Pavla Bojarová2,3, Karel Krenek2,3, Katharina Wetjen4, Kathrin Adamiak4, Helena Pelantová2, Karel Bezouska2,3, Lothar Elling1,4 and Vladimír Kren1,2

2 Institute of Microbiology, Center for Biocatalysis and Biotransformation, Academy of Sciences of the Czech Republic, Vídenská 1083, 14220 Prague 4
3 Department of Biochemistry, Faculty of Sciences, Charles University in Prague, Hlavova 8, 12840, Prague 2, Czech Republic
4 Laboratory for Biomaterials, Helmholtz Institute for Biomedical Engineering, RWTH Aachen University, Pauwelsstr. 20, 52074 Aachen, Germany

1 To whom correspondence should be addressed: Tel: +420-296442510; Fax: +420-296442509; e-mail: kren{at}biomed.cas.cz

Received on November 4, 2008; revised on January 7, 2009; accepted on January 23, 2009

Human placental β1,4-galactosyltransferase-I (EC 2.4.1.38 [EC] ) transfers the galactosyl moiety from UDP-Gal to various GlcNAc or Glc acceptors in vivo. Here, we describe the construction of its Y284L mutant as a His6propeptide-catβ4GalT1 construct, in which the Gal-transferase activity was totally abolished in favor of its GalNAc-transferase activity. We used this mutant in the synthesis of three mono- and bivalent LacdiNAc glycomimetics with good yields. These compounds proved to be powerful ligands of two activation receptors of natural killer cells, NKR-P1 and CD69. A synthetic bivalent tethered di-LacdiNAc is the best currently known precipitation agent for both of these receptors and has promising potential for the development of immunoactive glycodrugs.

Key words: enzymatic synthesis / glycomimetics / glycosyltransferase / LacdiNAc / natural killer cell


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.