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OGT cleaves Host Cell Factor C1, at one or more of 6 repeating 26 amino acid sequences. The TPR domain of OGT binds to the carboxyl terminal portion of an HCF1 proteolytic repeat so that the cleavage region is in the glycosyltransferase active site above uridine-diphosphate-GlcNAc [11] The large proportion of OGT complexed with HCF1 is necessary for HCF1 cleavage, and HCFC1 is required for OGT ...
O-GlcNAc (short for O-linked GlcNAc or O-linked β-N-acetylglucosamine) is a reversible enzymatic post-translational modification that is found on serine and threonine residues of nucleo cytoplasmic proteins. The modification is characterized by a β-glycosidic bond between the hydroxyl group of serine or threonine side chains and N ...
Two conserved enzymes control this glycosylation of serine and threonine: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). While OGT catalyzes the addition of O-GlcNAc to serine and threonine, OGA catalyzes the hydrolytic cleavage of O-GlcNAc from post-transitionally modified proteins. [14] OGA is a member of the family of hexosaminidases ...
O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational modification that occurs after the protein has been synthesised. In eukaryotes, it occurs in the endoplasmic reticulum, Golgi apparatus and occasionally in the ...
Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. [2] The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. Glycosylation is also present in the cytoplasm and nucleus as the O ...
The spike protein is a trimeric structure, with each subunit containing 22 N-glycosylation sites, making it an attractive target for vaccine search. [3] [4] Glycosylation, i.e., the addition of glycans (a generic name for monosaccharides and oligosaccharides ) to a protein, is one of the major post-translational modification of proteins ...
Glycation (non-enzymatic glycosylation) is the covalent attachment of a sugar to a protein, lipid or nucleic acid molecule. [1] Typical sugars that participate in glycation are glucose, fructose, and their derivatives. Glycation is the non-enzymatic process responsible for many (e.g. micro and macrovascular) complications in diabetes mellitus ...
Oligosaccharyltransferase or OST (EC 2.4.1.119) is a membrane protein complex that transfers a 14- sugar oligosaccharide from dolichol to nascent protein. It is a type of glycosyltransferase. The sugar Glc 3 Man 9 GlcNAc 2 (where Glc= Glucose, Man= Mannose, and GlcNAc= N -acetylglucosamine) is attached to an asparagine (Asn) residue in the ...