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

Expand all

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)

General

SBML | | PDF

SVG | | PPTX | SBGN

NEU2 hydrolyzes Neu5Ac from glycoconjugates

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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 Borsani, G, Preti, A, Ballabio, A, Rossi, E, Monti, E	Genomics	1999
15501818	Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition Tettamanti, G, Wakatsuki, S, Kato, R, Venerando, B, Monti, E, Fusi, P, Chavas, LM, Tringali, C	J. Biol. Chem.	2005