Reactome | ST8SIA1-6 transfer Neu5Ac to terminal Neu5Ac residues

ST8SIA1-6 transfer Neu5Ac to terminal Neu5Ac residues

Stable Identifier

R-HSA-4084978

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)
        
        ST8SIA1-6 transfer Neu5Ac to terminal Neu5Ac residues (Homo sapiens)

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ST8SIA1-6 transfer Neu5Ac to terminal Neu5Ac residues

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The alpha-2,8-sialyltransferases 1-6 (ST8SIA1-6) are involved in the production of gangliosides, glycoproteins and glycolipids. They transfer N-acetylneuraminate (Neu5Ac) to terminal Neu5Ac-yl groups of these glycoconjugates (Nakayama et al. 1996, Scheidegger et al. 1995, Lee et al. 1998, Angata et al. 2001, Kim et al. 1997). Once sialylated, glycoconjugates translocate to the plasma membrane by an unknown mechanism. For simplicity, Neu5Ac-R is shown in a generic form where R represents other sugars O-linked to proteins which can result in a large variability in glycoconjugate structures.

Literature References

PubMed ID	Title	Journal	Year
9199191	Molecular cloning and expression of human alpha2,8-sialyltransferase (hST8Sia V) Kim, YJ, Kim, KS, Do, S, Kim, CH, Kim, SK, Lee, YC	Biochem. Biophys. Res. Commun.	1997
7559389	A human STX cDNA confers polysialic acid expression in mammalian cells Scheidegger, EP, Sternberg, LR, Roth, J, Lowe, JB	J. Biol. Chem.	1995
9826427	Cloning and expression of cDNA for a human Sia alpha 2,3Gal beta 1, 4GlcNA:alpha 2,8-sialyltransferase (hST8Sia III) Lee, YC, Kim, YJ, Lee, KY, Kim, KS, Kim, BU, Kim, HN, Kim, CH, Do, SI	Arch. Biochem. Biophys.	1998
8631981	Expression cloning of a human GT3 synthase. GD3 AND GT3 are synthesized by a single enzyme Nakayama, J, Fukuda, MN, Hirabayashi, Y, Kanamori, A, Sasaki, K, Nishi, T, Fukuda, M	J. Biol. Chem.	1996
11279095	Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity Angata, K, Yen, TY, El-Battari, A, Macher, BA, Fukuda, M	J. Biol. Chem.	2001