NEU3 hydrolyzes Neu5Ac from glycoconjugates

Stable Identifier
R-HSA-4084994
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
18632803 Plasma membrane-associated sialidase as a crucial regulator of transmembrane signalling

Miyagi, T, Wada, T, Yamaguchi, K, Hata, K, Shiozaki, K

J. Biochem. 2008
10861246 Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane

Monti, E, Bassi, MT, Papini, N, Riboni, M, Manzoni, M, Venerando, B, Croci, G, Preti, A, Ballabio, A, Tettamanti, G, Borsani, G

Biochem J 2000
10405317 Cloning, expression, and chromosomal mapping of a human ganglioside sialidase

Wada, T, Yoshikawa, Y, Tokuyama, S, Kuwabara, M, Akita, H, Miyagi, T

Biochem. Biophys. Res. Commun. 1999
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
exo-alpha-sialidase activity of NEU3 [plasma membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created