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monosaccharides glycans transferases oligosaccharides protein-carbohydrate interactions

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Glycoconjugates and glycans are assembled by glycoslytransferases in reactions specific to the sugar donor and acceptor. These enzymes generally reside in the golgi compartament, with their catalytic domain facing the lumen. All GTs transfer from a sugar nucleotide to an acceptor, most often a sugar, or to a hydroxy group of a serine or theronine residue (as in the case of O-GalNAc transferases). The sugar may be a di- or mono-nucleotide (as in CMP-Sia).


These transferases may be grouped into conceptual families based on the biosynthetic pathways in which they participate, or the sugar donors in the reactions they catalyze.

Noteable Transferases:
b4-GalT (& Lactose Synthase)
α3-GalT
GlcNAcT
GlcUronylT

Available Structures:
Glycosyltransferase Gtfb (A. orientalis)
Spore Coat Polysaccharide Biosynthesis Protein Spsa (B. subtilsis)
α1-3-Galactosyltransferase (B. taurus)
b1-4-Galactosyltransferase (B. taurus)
α-Galactosyltransferase LgtC (N. meningitidis)
Glycogenin (O. cuniculus)
b-1,2-GlcNAc transferase I (O. cuniculus)
GlcNAc transferase MurG (E. coli)
Maltodextrin Phosphorylase MalP (E. coli)
Glycogen Phosphorylase (liver) (H. sapiens)
Glycogen Phosphorylase (muscle) (O. cuniculus)
Gkycogen Phosphorylase (S. cerevisiae)
β-1,3-glucuronyltransferase 3 (GlcU-TI) (H. sapiens)



Site designed and maintained by Aidan Ryan, LECB Structural Glycobiology Section, NCI Frederick, Maryland