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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 ...
Glycosyltransferase is a subcategory of EC 2.4 transferases that is involved in biosynthesis of disaccharides and polysaccharides through transfer of monosaccharides to other molecules. [40] An example of a prominent glycosyltransferase is lactose synthase which is a dimer possessing two protein subunits .
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 .
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 ...
Uridine 5'-diphospho-glucuronosyltransferase (UDP-glucuronosyltransferase, UGT) is a microsomal glycosyltransferase (EC 2.4.1.17) that catalyzes the transfer of the glucuronic acid component of UDP-glucuronic acid to a small hydrophobic molecule. This is a glucuronidation reaction. [2] [3] Alternative names: glucuronyltransferase; UDP ...
In enzymology, a scopoletin glucosyltransferase (EC 2.4.1.128) is an enzyme that catalyzes the chemical reaction UDP-glucose + scopoletin ⇌ {\displaystyle \rightleftharpoons } UDP + scopolin Thus, the two substrates of this enzyme are UDP-glucose and scopoletin , whereas its two products are UDP and scopolin .
In enzymology, an anthocyanin 3'-O-beta-glucosyltransferase (EC 2.4.1.238) is an enzyme that catalyzes the chemical reaction UDP-glucose + an anthocyanin ⇌ {\displaystyle \rightleftharpoons } UDP + an anthocyanin 3'-O-beta-D-glucoside
The product of this gene is a Golgi enzyme catalyzing an essential step in the conversion of oligomannose to complex N-glycans. The enzyme has the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain.