N-linked glycosylation, a protein modification system present in all domains of life, is
characterized by a high structural diversity of N-linked glycans found among different …

Glycosyltransferases catalyze glycosidic bond formation using sugar donors containing a
nucleoside phosphate or a lipid phosphate leaving group. Only two structural folds, GT-A …

At first glance, archaea and bacteria look alike; however, the composition of the archaeal
cell envelope is fundamentally different from the bacterial cell envelope. With just one …

Oligosaccharides together with oligonucleotides and oligopeptides comprise the three major
classes of natural biopolymers. Automated systems for oligonucleotide and oligopeptide …

Investigations into bacterial protein glycosylation continue to progress rapidly. It is now
established that bacteria possess both N-linked and O-linked glycosylation pathways that …

The attachment of glycans to asparagine residues of proteins is an abundant and highly
conserved essential modification in eukaryotes. The N-glycosylation process includes two …

Asparagine-linked glycosylation is a post-translational modification of proteins containing
the conserved sequence motif Asn-X-Ser/Thr. The attachment of oligosaccharides is …

Dilysine motifs in cytoplasmic domains of transmembrane proteins are signals for their
continuous retrieval from the Golgi back to the endoplasmic reticulum (El?). We describe a …

The multigene family of enzymes known as glycosyltransferases or popularly known as GTs
catalyze the addition of carbohydrate moiety to a variety of synthetic as well as natural …

Oligosaccharyltransferase (OST) catalyzes the transfer of a high-mannose glycan onto
secretory proteins in the endoplasmic reticulum. Mammals express two distinct OST …