Summary
N-acetyllactosamine synthase is a galactosyltransferase enzyme.[1][2][3][4][5][6] It is a component of lactose synthase[citation needed] This enzyme modifies the connection between two molecule UDP-galactose and N-actyl-D-glucosamine and generates two different molecules UDP and N-acetyllactosamine as products.[7] The main function of the enzyme is associated with the biosynthesis of glycoproteins and glycolipids in both human and animals.[7] In human, the activity of this enzyme can be found in Golgi apparatus.[7]
| N-acetyllactosamine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.90 | ||||||||
| CAS no. | 9054-94-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
It is classified under EC 2.4.1.90.
The lack of this enzyme leads to glycolysation[7][8][9] which is a serious neurological disease. The nature of the disease causes fluid in the brain, abnormal inflammatory response and abnormal bleeding issues.[7][8][9]
See also edit
References edit
- ^ Deshmukh DS, Bear WD, Soifer D (August 1978). "Isolation and characterization of an enriched Golgi fraction from rat brain". Biochimica et Biophysica Acta (BBA) - General Subjects. 542 (2): 284–95. doi:10.1016/0304-4165(78)90024-7. PMID 99178.
- ^ 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.
- ^ a b c d e 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.
- ^ a b 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.
- ^ a b 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.
External links edit
- N-acetyllactosamine+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
