Reactome | NEU2 hydrolyzes Neu5Ac from glycoconjugates

NEU2 hydrolyzes Neu5Ac from glycoconjugates

Stable Identifier

R-HSA-4085029

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

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)
        
        NEU2 hydrolyzes Neu5Ac from glycoconjugates (Homo sapiens)

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NEU2 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. NEU2 (cytosolic sialidase) hydrolyzes Neu5Ac from glycoconjugates with alpha2,3-, alpha2,6- or alpha2,8-linked terminal sialated residues in the cytosol (Monti et al. 1999, Chavas et al. 2005).

Literature References

PubMed ID	Title	Journal	Year
10191093	Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases Monti, E, Preti, A, Rossi, E, Ballabio, A, Borsani, G	Genomics	1999
15501818	Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition Chavas, LM, Tringali, C, Fusi, P, Venerando, B, Tettamanti, G, Kato, R, Monti, E, Wakatsuki, S	J. Biol. Chem.	2005