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Glycosylation also plays a role in cell-to-cell adhesion (a mechanism employed by cells of the immune system) via sugar-binding proteins called lectins, which recognize specific carbohydrate moieties. [2] Glycosylation is an important parameter in the optimization of many glycoprotein-based drugs such as monoclonal antibodies. [6]
The importance of N-linked glycosylation is becoming increasingly evident in the field of pharmaceuticals. [17] Although bacterial or yeast protein production systems have significant potential advantages such as high yield and low cost, problems arise when the protein of interest is a glycoprotein.
Diagram of yeast signaling pathways in response to glucose. Solid arrows represent transformations and/or translocations and dotted lines represent regulatory or catalytic influences. Glucose sensing and signaling in budding yeast is similar to the mammalian system in many ways. However, there are also significant differences.
Yeast OST is composed of eight different membrane-spanning proteins in three subcomplexes (one of them is OST4). [7] [8] These octomers do not form higher order oligomers, and three of the eight proteins are glycosylated themselves. [7] OST in mammals is known to have a similar composition. [9] [10]
The process of glycosylation (binding a carbohydrate to a protein) is a post-translational modification, meaning it happens after the production of the protein. [3] Glycosylation is a process that roughly half of all human proteins undergo and heavily influences the properties and functions of the protein. [3]
Nucleotide sugar metabolism is particularly well-studied in yeast, [5] fungal pathogens, [6] and bacterial pathogens, such as E. coli and Mycobacterium tuberculosis, since these molecules are required for the synthesis of glycoconjugates on the surfaces of these organisms.
Glycosylases in bacteria, yeast and humans [6] [7] E. coli B. cereus Yeast (S. cerevisiae) Human Type Substrates AlkA AlkE Mag1 MPG (N-methylpurine DNA glycosylase) monofunctional 3-meA(3-alkyladenine), hypoxanthine UDG Ung1 UNG monofunctional uracil Fpg Ogg1: hOGG1: bifunctional 8-oxoG (8-Oxoguanine), FapyG Nth Ntg1 hNTH1: bifunctional
A chemical glycosylation reaction involves the coupling of a glycosyl donor, to a glycosyl acceptor forming a glycoside. [ 1 ] [ 2 ] [ 3 ] If both the donor and acceptor are sugars, then the product is an oligosaccharide .