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Lactosylceramide alpha-2,3-sialyltransferase

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lactosylceramide alpha-2,3-sialyltransferase
Identifiers
EC no.2.4.99.9
CAS no.125752-90-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a lactosylceramide alpha-2,3-sialyltransferase (EC 2.4.99.9) is an enzyme that catalyzes the chemical reaction

CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D- glucosylceramide

Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and beta-D-galactosyl-1,4-beta-D-glucosylceramide, whereas its 3 products are CMP, alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D-, and glucosylceramide.

This enzyme belongs to the family of transferases, specifically those glycosyltransferases that do not transfer hexosyl or pentosyl groups. The systematic name of this enzyme class is CMP-N-acetylneuraminate:lactosylceramide alpha-2,3-N-acetylneuraminyltransferase. Other names in common use include cytidine monophosphoacetylneuraminate-lactosylceramide alpha2,3-, sialyltransferase, CMP-acetylneuraminate-lactosylceramide-sialyltransferase, CMP-acetylneuraminic acid:lactosylceramide sialyltransferase, CMP-sialic acid:lactosylceramide-sialyltransferase, cytidine monophosphoacetylneuraminate-lactosylceramide, sialyltransferase, ganglioside GM3 synthetase, GM3 synthase, GM3 synthetase, and SAT 1. This enzyme participates in glycosphingolipid biosynthesis - ganglioseries and glycan structures - biosynthesis 2.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2EX0 and 2EX1.

References

  • Basu S, Kaufman B, Roseman S (1973). "Enzymatic synthesis of glucocerebroside by a glucosyltransferase from embryonic chicken brain". J. Biol. Chem. 248 (4): 1388–94. PMID 4631392.
  • Fishman PH, Bradley RM, Henneberry RC (1976). "Butyrate-induced glycolipid biosynthesis in HeLa cells: properties of the induced sialyltransferase". Arch. Biochem. Biophys. 172 (2): 618–26. doi:10.1016/0003-9861(76)90116-8. PMID 4022.
  • Higashi H, Basu M, Basu S (1985). "Biosynthesis in vitro of disialosylneolactotetraosylceramide by a solubilized sialyltransferase from embryonic chicken brain". J. Biol. Chem. 260 (2): 824–8. PMID 3838172.