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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 .
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-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 ...
New hope could be on the horizon for ALS patients in the form of a “breakthrough" drug, researchers say. Neuvivo is seeking approval for an experimental medication for the neurological condition.
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.
Glycosylation is the reaction in which a carbohydrate (or ' glycan '), i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule (a glycosyl acceptor) in order to form a glycoconjugate. In biology (but not always in chemistry), glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation ...
Galectin. Structure of human galectin-9 in complex with N -acetyllactosamine dimer, clearly showing the two carbohydrate binding sites. Galectins are a class of proteins that bind specifically to β-galactoside sugars, such as N -acetyllactosamine (Galβ1-3GlcNAc or Galβ1-4GlcNAc), which can be bound to proteins by either N-linked or O-linked ...
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 ...