UDP-glycosyltransferases (UGTs) are the most studied glycosyltransferases, and belong to large GT1 family performing key roles in antibiotic synthesis, development of bacterial glycosyltransferase inhibitors, animal inflammation. They transfer glycosyl groups from nucleotide UDP-sugars (UDP-glucose, UDP-galactose, UDP-xylose, UDP-rhamnose) acceptors including saccharides, proteins, lipids, seco...

Natural product C-glycosyltransferases are forming the rare C-glycosidic bonds that represent a synthetic challenge.

Glycosyltransferases, the enzymes that build oligosaccharides and glycoconjugates, have received much interest in recent years owing to their biological functions and their potential uses in biotechnology. Despite the fact that many glycosyltransferases recognize similar donor or acceptor substrates, there is surprisingly limited sequence identity between different classes. On the one hand, the...

BACKGROUND Glycosylation is the most frequent posttranslational modification of proteins and lipids influencing inter- and intracellular communication and cell adhesion. Altered glycosylation patterns are characteristically observed in tumour cells. Normal and altered carbohydrate chains are transferred to their acceptor structures via glycosyltransferases. Here, we present the correlation betw...

Glycosyltransferases catalyze the reaction between an activated sugar donor and an acceptor to form a new glycosidic linkage. Glycosyltransferases are responsible for the assembly of oligosaccharides in vivo and are also important for the in vitro synthesis of these biomolecules. However, the functional identification and characterization of new glycosyltransferases is difficult and tedious. Th...

Fifty-one human glycosyltransferases were expressed in Saccharomyces cerevisiae as immobilized enzymes and were assayed for enzymatic activities. The stem and catalytic regions of sialyl-, fucosyl-, galactosyl-, N-acetylgalactosaminyl-, and N-acetylglucosaminyltransferases were fused with yeast cell wall Pir proteins, which anchor glycosyltransferases at the yeast cell wall glucan. More than 75...

Glycosylation is one of the major post-translational modification processes essential for expression and function of many proteins. It has been estimated that 1% of the open reading frames of a genome is dedicated to glycosylation. Many different enzymes are involved in glycosylation, such as glycosyltransferases and glycosidases. Traditionally, glycosyltransferases are classified based on thei...

The vast majority of eukaryotes (fungi, plants, animals, slime mold, and euglena) synthesize Asn-linked glycans (Alg) by means of a lipid-linked precursor dolichol-PP-GlcNAc2Man9Glc3. Knowledge of this pathway is important because defects in the glycosyltransferases (Alg1-Alg12 and others not yet identified), which make dolichol-PP-glycans, lead to numerous congenital disorders of glycosylation...