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.
Wu, ZL, Prather, B, Jiang, W, Machacek, M, Ethen, CM
Takashima, S, Tsuji, S, Tsujimoto, M
Teintenier-Lelièvre, M, Harduin-Lepers, A, Mir, AM, Delannoy, P, Samyn-Petit, B, Cerutti, M, Krzewinski-Recchi, MA, Juliant, S, Julien, S, Montiel, MD
beta-galactoside alpha-2,6-sialyltransferase activity of ST6GAL1,2 [Golgi membrane]
© 2022 Reactome
