ST6GAL1,2 transfer Neu5Ac to terminal Gal (alpha-2,6 link)

Stable Identifier
Reaction [transition]
Homo sapiens
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The beta-galactoside alpha-2,6-sialyltransferases 1 and 2 (ST6GAL1,2) are able to transfer a sialic acid (Neu5Ac) moiety to the terminal galactosyl (Gal-R) residue of O-glycosylated proteins and some gangliosides. Neu5Ac is added to Gal-R via an alpha-2,6 linkage (Wu et al. 2011, Takashima et al. 2002, Krzewinski-Recchi et al. 2003). Once sialylated, glycoconjugates translocate to the plasma membrane by an unknown mechanism. For simplicity, Gal is shown in a generic form where R represents other sugars O-linked to proteins. Highest activity is observed toward oligosaccharides that have the Gal-beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups.

Literature References
PubMed ID Title Journal Year
21081508 Universal phosphatase-coupled glycosyltransferase assay

Wu, ZL, Prather, B, Jiang, W, Machacek, M, Ethen, CM

Glycobiology 2011
12235148 Characterization of the second type of human beta-galactoside alpha 2,6-sialyltransferase (ST6Gal II), which sialylates Galbeta 1,4GlcNAc structures on oligosaccharides preferentially. Genomic analysis of human sialyltransferase genes

Takashima, S, Tsuji, S, Tsujimoto, M

J. Biol. Chem. 2002
12603328 Identification and functional expression of a second human beta-galactoside alpha2,6-sialyltransferase, ST6Gal II

Teintenier-Lelièvre, M, Harduin-Lepers, A, Mir, AM, Delannoy, P, Samyn-Petit, B, Cerutti, M, Krzewinski-Recchi, MA, Juliant, S, Julien, S, Montiel, MD

Eur J Biochem 2003
Catalyst Activity

beta-galactoside alpha-2,6-sialyltransferase activity of ST6GAL1,2 [Golgi membrane]

Orthologous Events
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