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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 ...
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.
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 ...
80908 Ensembl ENSG00000175164 ENSG00000281879 ENSMUSG00000015787 UniProt P16442 P38649 RefSeq (mRNA) NM_020469 NM_030718 NM_001290444 RefSeq (protein) NP_065202 NP_001277373 NP_109643 Location (UCSC) Chr 9: 133.23 – 133.28 Mb Chr 2: 26.73 – 26.75 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Histo-blood group ABO system transferase is an enzyme with glycosyltransferase activity ...
The antibody has a three-dimensional structure with beta pleated sheet and alpha helices. [5] The antibody folds so the variable regions form three loops with the framework regions folded into one another and the CDR regions on the tips of each of these loops in direct contact with the antigen.
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.
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 .
Beta-glucosyltransferase is an enzyme, or more specifically an inverting glycosyltransferase (GT). In other words, it transfers glucose from uridine diphospho-glucose (UDPglucose) to an acceptor, modified DNA through beta-Glycosidic bond. The role of the enzyme is to protect the infecting viral DNA from the bacteria's restriction enzymes ...