Lactosylceramide alpha-2,3-sialyltransferase
lactosylceramide alpha-2,3-sialyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.4.99.9 | ||||||||
CAS no. | 125752-90-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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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 and , whereas its 3 products are CMP, , 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 and .
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.
- EC 2.4.99
- Enzymes of known structure
- EC 2.4 stubs