N-acetyllactosamine synthase

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 number2.4.1.90
CAS number9054-94-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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

References
  1. 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.
  2. 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.
  3. 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. 43. pp. 411–90. doi:10.1002/9780470122884.ch5. ISBN 9780470122884. PMID 812340.
  4. 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. PMID 6201486.
  5. 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. PMID 4392041.
  6. Taniguchi N, Honke K, Fukuda M (2002). Handbook of glycosyltransferases and related genes (1st ed.). Springer. ISBN 443170311X.
  7. Schomburg D, Schomburg I, Chang A, eds. (2006). Springer Handbook of Enzymes. Springer Handbook of Enzymes. 27. doi:10.1007/3-540-30439-8. ISBN 978-3-540-26583-2.
  8. 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.
  9. 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.


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