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Glycosyltransferases are enzymes that establish natural glycosidic linkages. They catalyze the transfer of saccharide moieties from an activated nucleotide sugar to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur-based.
Lactose synthase is an enzyme that generates lactose from glucose and UDP-galactose.
The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.
In enzymology, a ganglioside galactosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a lactosylceramide 4-alpha-galactosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a monogalactosyldiacylglycerol synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a procollagen galactosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a sn-glycerol-3-phosphate 2-alpha-galactosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine diphosphorylase is an enzyme that catalyzes the chemical reaction
Beta-1,4-galactosyltransferase 1 is an enzyme that in humans is encoded by the B4GALT1 gene.
UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that in humans is encoded by the DPAGT1 gene.
UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the B3GALNT1 gene.
Beta-1,4-galactosyltransferase 7 also known as galactosyltransferase I is an enzyme that in humans is encoded by the B4GALT7 gene. Galactosyltransferase I catalyzes the synthesis of the glycosaminoglycan-protein linkage in proteoglycans. Proteoglycans in turn are structural components of the extracellular matrix that is found between cells in connective tissues.
Beta-1,4-galactosyltransferase 2 is an enzyme that in humans is encoded by the B4GALT2 gene.
Beta-1,4-galactosyltransferase 3 is an enzyme that in humans is encoded by the B4GALT3 gene.
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. In eukaryotes, it occurs in the endoplasmic reticulum, Golgi apparatus and occasionally in the cytoplasm; in prokaryotes, it occurs in the cytoplasm. Several different sugars can be added to the serine or threonine, and they affect the protein in different ways by changing protein stability and regulating protein activity. O-glycans, which are the sugars added to the serine or threonine, have numerous functions throughout the body, including trafficking of cells in the immune system, allowing recognition of foreign material, controlling cell metabolism and providing cartilage and tendon flexibility. Because of the many functions they have, changes in O-glycosylation are important in many diseases including cancer, diabetes and Alzheimer's. O-glycosylation occurs in all domains of life, including eukaryotes, archaea and a number of pathogenic bacteria including Burkholderia cenocepacia, Neisseria gonorrhoeae and Acinetobacter baumannii.
(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:1-O-(O- - -O-beta-D-galactopyranosyl- -beta-D-glucopyranosyl)-ceramide 4-beta-N-acetyl-D-galactosaminyltransferase. This enzyme catalyses the following chemical reaction:
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:3-(alpha-D-mannosyl)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction
Glucosylceramide beta-1,4-galactosyltransferase is an enzyme with systematic name UDP-alpha-D-galactose:beta-D-glucosyl-(1<->1)-ceramide 4-beta-D-galactosyltransferase. This enzyme catalyses the following chemical reaction
References
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- ↑ Helting T, Erbing B (January 1973). "Galactosyltransfer in mouse mastocytoma: purification and properties of N-acetyllactosamine synthetase". Biochimica et Biophysica Acta (BBA) - Enzymology. 293 (1): 94–104. doi:10.1016/0005-2744(73)90379-3. PMID 4631039.
- ↑ Hill RL, Brew K (1975). "Lactose synthetase". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology and Related Areas of Molecular Biology. Vol. 43. pp. 411–90. doi:10.1002/9780470122884.ch5. ISBN 9780470122884. PMID 812340.
- ↑ Humphreys-Beher MG (May 1984). "Isolation and characterization of UDP-galactose:N-acetylglucosamine 4 beta-galactosyltransferase activity induced in rat parotid glands treated with isoproterenol". The Journal of Biological Chemistry. 259 (9): 5797–802. doi: 10.1016/S0021-9258(18)91084-7 . PMID 6201486.
- ↑ Schachter H, Jabbal I, Hudgin RL, Pinteric L, McGuire EJ, Roseman S (March 1970). "Intracellular localization of liver sugar nucleotide glycoprotein glycosyltransferases in a Golgi-rich fraction". The Journal of Biological Chemistry. 245 (5): 1090–100. doi: 10.1016/S0021-9258(18)63293-4 . PMID 4392041.
- ↑ Taniguchi N, Honke K, Fukuda M (2002). Handbook of glycosyltransferases and related genes (1st ed.). Springer. ISBN 443170311X.
- 1 2 3 4 5 Schomburg D, Schomburg I, Chang A, eds. (2006). Springer Handbook of Enzymes. Vol. 27. doi:10.1007/3-540-30439-8. ISBN 978-3-540-26583-2.
- 1 2 Hansske B, Thiel C, Lübke T, Hasilik M, Höning S, Peters V, et al. (March 2002). "Deficiency of UDP-galactose:N-acetylglucosamine beta-1,4-galactosyltransferase I causes the congenital disorder of glycosylation type IId". The Journal of Clinical Investigation. 109 (6): 725–33. doi:10.1172/jci0214010. PMC 150909 . PMID 11901181.
- 1 2 Reily C, Stewart TJ, Renfrow MB, Novak J (June 2019). "Glycosylation in health and disease". Nature Reviews. Nephrology. 15 (6): 346–366. doi:10.1038/s41581-019-0129-4. PMC 6590709 . PMID 30858582.
