ExplorEnz: EC 3.2.1.129

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3.2.1.129

Accepted name:

endo-α-sialidase

Reaction:

Endohydrolysis of (2→8)-α-sialosyl linkages in oligo- or poly(sialic) acids

Other name(s):

endo-N-acylneuraminidase; endoneuraminidase; endo-N-acetylneuraminidase; poly(α-2,8-sialosyl) endo-N-acetylneuraminidase; poly(α-2,8-sialoside) α-2,8-sialosylhydrolase; endosialidase; endo-N

Systematic name:

polysialoside (2→8)-α-sialosylhydrolase

Comments:

Although the name endo-N-acetylneuraminidase has also been used for this enzyme, this is misleading since its activity is not restricted to acetylated substrates. An exo-α-sialidase activity is listed as EC 3.2.1.18 exo-α-sialidase. See also EC 4.2.2.15 anhydrosialidase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 91195-87-8

References:

1.	Finne, J., Mäkelä, P.H. Cleavage of the polysialosyl units of brain glycoproteins by a bacteriophage endosialidase. Involvement of a long oligosaccharide segment in molecular interactions of polysialic acid. J. Biol. Chem. 260 (1985) 1265–1270. [PMID: 3968060]
2.	Hallenbeck, P.C., Vimr, E.R., Yu, F., Bassler, B. and Troy, F.A. Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-α-2,8-sialosyl carbohydrate units. J. Biol. Chem. 262 (1987) 3553–3561. [PMID: 3546309]
3.	Kitakima, K., Inoue, S., Inoue, Y. and Troy, F.A. Use of a bacteriophage-derived endo-N-acetylneuraminidase and an equine antipolysialyl antibody to characterize the polysialyl residues in salmonid fish egg polysialoglycoproteins. Substrate and immunospecificity studies. J. Biol. Chem. 263 (1988) 18269–18276. [PMID: 3142874]
4.	Kwiatkowski, B., Boscheck, B., Thicle, H. and Stirm, S. Endo-N-acetylneuraminidase associated with bacteriophage particles. J. Virol. 43 (1982) 697–704. [PMID: 7109038]
5.	Pelkonen, S., Pelkonen, J. and Finne, J. Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins. J. Virol. 65 (1989) 4409–4416. [PMID: 2778882]
6.	Tombinson, S. and Taylor, P.W. Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide. J. Virol. 55 (1985) 374–378. [PMID: 3894684]
7.	Cabezas, J.A. Some questions and suggestions on the type references of the official nomenclature (IUB) for sialidase(s) and endosialidase. Biochem. J. 278 (1991) 311–312. [PMID: 1883340]

[EC 3.2.1.129 created 1990, modified 1999]