Beta-galactoside alpha-2,6-sialyltransferase
beta-galactoside alpha-2,6-sialyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.4.99.1 | ||||||||
CAS no. | 9075-81-4 | ||||||||
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 beta-galactoside alpha-2,6-sialyltransferase (EC 2.4.99.1) is an enzyme that catalyzes the chemical reaction
- CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D- glucosamine
Thus, the two substrates of this enzyme are CMP-N-acetylneuraminate and beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine, whereas its three products are CMP, alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl-1,4-N-acetyl-beta-D-, and glucosamine.
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:beta-D-galactosyl-1,4-N-acetyl-beta-D-glucos amine alpha-2,6-N-acetylneuraminyltransferase. This enzyme participates in n-glycan biosynthesis and glycan structures - biosynthesis 1.
References
- Bartholomew BA, Jourdian GW, Roseman S (1973). "The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum". J. Biol. Chem. 248 (16): 5751–62. doi:10.1016/S0021-9258(19)43568-0. PMID 4723915.
- Hickman J, Ashwell G, Morell AG, van den Hamer CJ, Scheinberg IH (1970). "Physical and chemical studies on ceruloplasmin. 8. Preparation of N-acetylneuraminic acid-1-14C-labeled ceruloplasmin". J. Biol. Chem. 245 (4): 759–66. doi:10.1016/S0021-9258(18)63329-0. PMID 4313609.
- Paulson JC, Beranek WE, Hill RL (1977). "Purification of a sialyltransferase from bovine colostrum by affinity chromatography on CDP-agarose". J. Biol. Chem. 252 (7): 2356–62. doi:10.1016/S0021-9258(17)40562-X. PMID 849932.
- Schachter H, Narasimhan S, Gleeson P, Vella G (1983). Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. Vol. 98. pp. 98–134. doi:10.1016/0076-6879(83)98143-0. ISBN 978-0-12-181998-9. PMID 6366476.
- Spiro MJ, Spiro RG (1968). "Glycoprotein biosynthesis: studies on thyroglobulin. Thyroid sialyltransferase". J. Biol. Chem. 243 (24): 6520–8. doi:10.1016/S0021-9258(18)97805-1. PMID 5726897.