KEGG ENZYME: 3.2.1.129

ENZYME: 3.2.1.129

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

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)
DOI:10.1128/JVI.43.2.697-704.1982

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)
DOI:10.1128/JVI.63.10.4409-4416.1989

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)
DOI:10.1128/JVI.55.2.374-378.1985

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)
DOI:10.1042/bj2780311

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

All links

Protein sequence (61)   
   UniProt (20)   
   SWISS-PROT (2)   
   RefSeq(pep) (10)   
   PDBSTR (27)   
   PMD (2)   
DNA sequence (55)   
   RefSeq(nuc) (9)   
   GenBank (24)   
   EMBL (22)   
3D Structure (8)   
   PDB (8)   
Protein domain (12)   
   InterPro (12)   
All databases (136)   

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