KEGG   ENZYME: 3.2.1.129Help
Entry
EC 3.2.1.129                Enzyme                                 

Name
endo-alpha-sialidase;
endo-N-acylneuraminidase;
endoneuraminidase;
endo-N-acetylneuraminidase;
poly(alpha-2,8-sialosyl) endo-N-acetylneuraminidase;
poly(alpha-2,8-sialoside) alpha-2,8-sialosylhydrolase;
endosialidase;
endo-N
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
polysialoside (2->8)-alpha-sialosylhydrolase
Reaction(IUBMB)
Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids
Comment
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-alpha-sialidase activity is listed as EC 3.2.1.18 exo-alpha-sialidase. See also EC 4.2.2.15 anhydrosialidase.
History
EC 3.2.1.129 created 1990, modified 1999
Reference
1  [PMID:3968060]
  Authors
Finne J, Makela PH.
  Title
Cleavage of the polysialosyl units of brain glycoproteins by a bacteriophage endosialidase. Involvement of a long oligosaccharide segment in molecular interactions of polysialic acid.
  Journal
J Biol Chem 260:1265-70 (1985)
Reference
2  [PMID:3546309]
  Authors
Hallenbeck PC, Vimr ER, Yu F, Bassler B, Troy FA.
  Title
Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units.
  Journal
J Biol Chem 262:3553-61 (1987)
Reference
3  [PMID:3142874]
  Authors
Kitajima K, Inoue S, Inoue Y, Troy FA.
  Title
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.
  Journal
J Biol Chem 263:18269-76 (1988)
Reference
4  [PMID:7109038]
  Authors
Kwiatkowski B, Boschek B, Thiele H, Stirm S.
  Title
Endo-N-acetylneuraminidase associated with bacteriophage particles.
  Journal
J Virol 43:697-704 (1982)
Reference
5  [PMID:2778882]
  Authors
Pelkonen S, Pelkonen J, Finne J.
  Title
Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins.
  Journal
J Virol 63:4409-16 (1989)
Reference
6  [PMID:3894684]
  Authors
Tomlinson S, Taylor PW.
  Title
Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide.
  Journal
J Virol 55:374-8 (1985)
Reference
7  [PMID:1883340]
  Authors
Cabezas JA.
  Title
Some questions and suggestions on the type references of the official nomenclature (IUB) for sialidase(s) and endosialidase.
  Journal
Biochem J 278 ( Pt 1):311-2 (1991)
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.129
IUBMB Enzyme Nomenclature: 3.2.1.129
ExPASy - ENZYME nomenclature database: 3.2.1.129
BRENDA, the Enzyme Database: 3.2.1.129
CAS: 91195-87-8

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