EC 3.2.1.129 - Endo-α-sialidase

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IntEnz Enzyme Nomenclature
EC 3.2.1.129

Names

Accepted name:
endo-α-sialidase
Other names:
α-2,8-sialosylhydrolase
endo-N-acetylneuraminidase [misleading]
endo-N-acylneuraminidase
endoneuraminidase
endosialidase
poly(α-2,8-sialoside) α-2,8-sialosylhydrolase
poly(α-2,8-sialosyl) endo-N-acetylneuraminidase
Systematic name:
polysialoside (2→8)-α-sialosylhydrolase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0016996
UniProtKB/Swiss-Prot:

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: 1265-1270 (1985). [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: 3553-3561 (1987). [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: 18269-18276 (1988). [PMID: 3142874]
  4. Kwiatkowski, B., Boscheck, B., Thicle, H. and Stirm, S.
    Endo-N-acetylneuraminidase associated with bacteriophage particles.
    J. Virol. 43: 697-704 (1982). [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: 4409-4416 (1989). [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: 374-378 (1985). [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: 311-312 (1991). [PMID: 1883340]

[EC 3.2.1.129 created 1990, modified 1999]