Predictable Enzymatic Glycosylation

Enzymatic N-glycosylation of synthetic Asn--X--Thr containing peptides.

The role of polyprenol sugar derivatives in the biosynthesis of certain eukaryotic glycoproteins has been partly described [ 11. Recently lipid pyrophospho-oligosaccharides, postulated as necessary intermediates to initiate N-glycosylation, were shown, when supplied to microsomes, to be effective donors to proteinic acceptors presenting at least one vacant Asn-X-zk sequence: unfolded forms of p...

Evidence for non-enzymatic glycosylation of Escherichia coli chromosomal DNA.

We have recently shown that the process of non-enzymatic glycosylation (glycation) takes place in Escherichia coli under physiological conditions and affects both recombinant and endogenous bacterial proteins. In this study, we further demonstrate that E. coli chromosomal DNA is also subjected to glycation under physiological growth conditions. The E. coli DNA accumulates early glycation (Amado...

the effect of some flavonoids on in-vitro non-enzymatic glycosylation of proteins

introduction: non-enzymatic glycosylation of proteins which is the major cause of diabetic complications, cardiovascular diseases retinopathy, nephropathy and neuropathy can effectively be inhibted by antioxidants. materials and method: the antioxidant effects of several flavonoids, such as rutin, kaempferol, quercetin, apigenin, naringin, morin and biochanin a were studied  on glycosylation of...

Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.

The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies. Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known. Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in ...

Efficient enzymatic glycosylation of peptides and oligosaccharides from GalNAc and UTP.