Reactome | NEU3 hydrolyzes Neu5Ac from glycoconjugates

NEU3 hydrolyzes Neu5Ac from glycoconjugates

Stable Identifier

R-HSA-4084994

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

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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)
        
        NEU3 hydrolyzes Neu5Ac from glycoconjugates (Homo sapiens)

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NEU3 hydrolyzes Neu5Ac from glycoconjugates

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Sialidases 1-4 (NEU1-4, neuraminidases, receptor-destroying enzymes, RDEs) hydrolyze sialic acids (N-acetylneuraminic acid, Neu5Ac) to produce asialo compounds, a step in the degradation process of glycoproteins and gangliosides and are expressed in a variety of cellular locations. NEU3 localizes to the plasma membrane and hydrolyses Neu5Ac especially from gangliosides with alpha2,3- or alpha2,8-linkages present in the lipid bilayer (Wada et al. 1999, Monti et al. 2000). By regulating the composition of the lipid bilayer, NEU3 has been identified as an important regulator of trans-membrane signaling (Miyagi et al. 2008).

Literature References

PubMed ID	Title	Journal	Year
10861246	Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane Borsani, G, Preti, A, Manzoni, M, Papini, N, Venerando, B, Tettamanti, G, Bassi, MT, Ballabio, A, Croci, G, Riboni, M, Monti, E	Biochem J	2000
18632803	Plasma membrane-associated sialidase as a crucial regulator of transmembrane signalling Hata, K, Wada, T, Miyagi, T, Shiozaki, K, Yamaguchi, K	J. Biochem.	2008
10405317	Cloning, expression, and chromosomal mapping of a human ganglioside sialidase Miyagi, T, Wada, T, Tokuyama, S, Akita, H, Yoshikawa, Y, Kuwabara, M	Biochem. Biophys. Res. Commun.	1999