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Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...
Glucosyltransferases are a type of glycosyltransferase that enable the transfer of glucose. [1] Examples include: glycogen synthase; glycogen phosphorylase; They are categorized under EC number 2.4.1.
N-glycosyltransferase is an enzyme in prokaryotes which transfers individual hexoses onto asparagine sidechains in substrate proteins, using a nucleotide-bound intermediary, within the cytoplasm. They are distinct from regular N -glycosylating enzymes , which are oligosaccharyltransferases that transfer pre-assembled oligosaccharides .
Histo-blood group ABO system transferase is an enzyme with glycosyltransferase activity, which is encoded by the ABO gene in humans. [5] [6] It is ubiquitously expressed in many tissues and cell types. [7] ABO determines the ABO blood group of an individual by modifying the oligosaccharides on cell surface glycoproteins. Variations in the ...
In enzymology, a 1,4-alpha-glucan 6-alpha-glucosyltransferase (EC 2.4.1.24) is an enzyme that catalyzes the chemical reaction that transfers an alpha-D-glucosyl residue in a 1,4-alpha-D-glucan to the primary hydroxyl group of glucose or 1,4-alpha-D-glucan. This enzyme belongs to the family of glycosyltransferases, specifically the ...
UDP-glucose is used in nucleotide sugar metabolism as an activated form of glucose, a substrate for enzymes called glucosyltransferases. [1]UDP-glucose is a precursor of glycogen and can be converted into UDP-galactose and UDP-glucuronic acid, which can then be used as substrates by the enzymes that make polysaccharides containing galactose and glucuronic acid.
In enzymology, a 4-alpha-glucanotransferase (EC 2.4.1.25) is an enzyme that catalyzes a chemical reaction that transfers a segment of a 1,4-alpha-D-glucan to a new position in an acceptor carbohydrate, which may be glucose or a 1,4-alpha-D-glucan. This enzyme belongs to the family of glycosyltransferases, specifically
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 ...