Glycobiology Advance Access originally published online on February 5, 2007
Glycobiology 2007 17(5):7G-9G; doi:10.1093/glycob/cwm013
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Letter to the Glyco-Forum: Catalytic domains of glycosyltransferases with ‘add-on’ domains
2 Structural Glycobiology Section, CCR Nanobiology Program
3 Basic Science Program, SAIC-Frederick, Inc., Center for Cancer Research, National Cancer Institute at Frederick, Building 469, Room 221, Frederick, MD, 21702
1 Tel: +1 301 846 1934; fax: +1 301 846 7149; e-mail : qasba@helix.nih.gov
| The first 10% of the full text of this article appears below. |
Glycosyltransferases (GTs) belong to a large family of enzymes that are involved in the synthesis of oligosaccharide moieties of glycoproteins, glycolipids, and proteoglycans and have been assembled in a CAZy database (http://www.cazy.org). In the eukaryotic cells, most of these enzymes are Golgi-resident type II membrane proteins with a cytoplasmic domain, a transmembrane domain, and a stem region with a catalytic domain facing the Golgi-lumen, which transfers a sugar moiety from an activated sugar nucleotide donor to an acceptor molecule with either retention or inversion of the stereochemistry at the C1 position of the donor sugar.
Crystal structures of the catalytic domain of several GT enzymes have been recently reported. Most of these structures fall into a GT-A fold which has an N-terminal Rossmann-like nucleotide-binding domain and a C-terminal acceptor-binding