Glycosyltransferases (GTFs, Gtfs) are compounds (EC 2.4) that build up common glycosidic linkages. They catalyze the exchange of saccharide moieties from an actuated nucleotide sugar (otherwise called the "glycosyl donorr") to a nucleophilic glycosyl acceptor particle, the nucleophile of which can be oxygen-carbon-, nitrogen-, or sulfur-based. The consequence of glycosyl exchange can be a starch, glycoside, oligosaccharide, or a polysaccharide. Some glycosyltransferases catalyze exchange to inorganic phosphate or water. Glycosyl can also occur to protein residues, more often to tyrosine, serine, or threonine to give O-connected glycoproteins, or to asparagine to give N-connected glycoproteins. Mannosyl gatherings might be exchanged to tryptophan to create C-mannosyl tryptophan, which is moderately inexhaustible in eukaryotes. Transferases may likewise utilize lipids as an acceptor, framing glycolipids, and even utilize lipid-linked sugar phosphate donors, for example, dolichol phosphates. Glycosyltransferases that utilize sugar nucleotide donars are Leloir compounds, after Luis F. Leloir, the researcher who found the main sugar nucleotide and who got the 1970 Nobel Prize in Chemistry for his work on starch digestion. Glycosyltransferases that utilizes non-nucleotide donors, for example, dolichol or polyprenol pyrophosphate are non-Leloir glycosyltransferases. Warm blooded creatures utilize just 9 sugar nucleotide contributors for glycosyltransferases: UDP-glucose, UDP-galactose, UDP-GlcNAc, UDP-GalNAc, UDP-xylose, UDP-glucuronic corrosive, GDP-mannose, GDP-fucose, and CMP-sialic corrosive. The phosphate(s) of these contributor atoms are normally organized by divalent cations, for example, manganese, anyway metal autonomous catalysts exist. Numerous glycosyltransferases are single-pass transmembrane proteins, and they are typically secured to layers of Golgi contraption.
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