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Protein O-GlcNAc transferase also known as OGT or O-linked N-acetylglucosaminyltransferase is an enzyme (EC 2.4.1.255) that in humans is encoded by the OGT gene. [ 5 ] [ 6 ] OGT catalyzes the addition of the O -GlcNAc post-translational modification to proteins .
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 ...
The result of glycosyl transfer can be a carbohydrate, glycoside, oligosaccharide, or a polysaccharide. Some glycosyltransferases catalyse transfer to inorganic phosphate or water . Glycosyl transfer can also occur to protein residues, usually to tyrosine , serine , or threonine to give O-linked glycoproteins , or to asparagine to give N-linked ...
Allosteric regulation. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.