In enzymology, a lactosylceramide alpha-2,6-N-sialyltransferase (EC 2.4.99.11) is an enzyme that catalyzes the chemical reaction
| lactosylceramide alpha-2,6-N-sialyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.99.11 | ||||||||
| CAS no. | 55071-95-9 | ||||||||
| 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 | ||||||||
| |||||||||
- CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide CMP + alpha-N-acetylneuraminyl-2,6-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-2,6-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-2,6-N-acetylneuraminyltransferase. Other names in common use include cytidine monophosphoacetylneuraminate-lactosylceramide, sialyltransferase, CMP-acetylneuraminate-lactosylceramide-sialyltransferase, CMP-N-acetylneuraminic acid:lactosylceramide sialyltransferase, CMP-sialic acid:lactosylceramide sialyltransferase, cytidine monophosphoacetylneuraminate-lactosylceramide, and sialyltransferase.
References
edit- Albarracin I, Lassaga FE, Caputto R (1988). "Purification and characterization of an endogenous inhibitor of the sialyltransferase CMP-N-acetylneuraminate: lactosylceramide alpha 2,6-N-acetylneuraminyltransferase (EC 2.4.99.-)". Biochem. J. 254 (2): 559–65. PMC 1135114. PMID 2460092.
- Landa CA, Maccioni HJ, Arce A, Caputto R (1977). "The biosynthesis of brain gangliosides. Separation of membranes with different ratios of ganglioside sialylating activity to gangliosides". Biochem. J. 168 (3): 325–32. PMC 1183776. PMID 606237.
