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

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

Stable Identifier

R-HSA-4085033

Type

Reaction [transition]

Species

Homo sapiens

Compartment

Golgi membrane, Golgi lumen

Locations in the PathwayBrowser

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Metabolism of proteins (Homo sapiens)

- Post-translational protein modification (Homo sapiens)
  - Asparagine N-linked glycosylation (Homo sapiens)
    - Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein (Homo sapiens)
      - Synthesis of substrates in N-glycan biosythesis (Homo sapiens)
        
        Sialic acid metabolism (Homo sapiens)
        
        ST6GAL1,2 transfer Neu5Ac to terminal Gal (alpha-2,6 link) (Homo sapiens)

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

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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
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
21081508	Universal phosphatase-coupled glycosyltransferase assay Wu, ZL, Ethen, CM, Prather, B, Machacek, M, Jiang, W	Glycobiology	2011
12603328	Identification and functional expression of a second human beta-galactoside alpha2,6-sialyltransferase, ST6Gal II Krzewinski-Recchi, MA, Julien, S, Juliant, S, Teintenier-Lelièvre, M, Samyn-Petit, B, Montiel, MD, Mir, AM, Cerutti, M, Harduin-Lepers, A, Delannoy, P	Eur J Biochem	2003