Endo-alpha-sialidase

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Endo-alpha-sialidase (EC 3.2.1.129, 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) is an enzyme with systematic name polysialoside (2->8)-alpha-sialosylhydrolase.^[1]^[2]^[3]^[4]^[5]^[6]^[7] This enzyme catalyses the following chemical reaction:

Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids

References

↑ Finne, J., Mäkelä, P.H. (1985). "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 (2): 1265–1270. PMID 3968060.
↑ Hallenbeck, P.C., Vimr, E.R., Yu, F., Bassler, B. and Troy, F.A. (1987). "Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-α-2,8-sialosyl carbohydrate units". J. Biol. Chem. 262 (8): 3553–3561. PMID 3546309.
↑ Kitakima, K., Inoue, S., Inoue, Y. and Troy, F.A. (1988). "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 (34): 18269–18276. PMID 3142874.
↑ Kwiatkowski, B., Boscheck, B., Thicle, H. and Stirm, S. (1982). "Endo-N-acetylneuraminidase associated with bacteriophage particles". J. Virol. 43 (2): 697–704. PMID 7109038.
↑ Pelkonen, S., Pelkonen, J. and Finne, J. (1989). "Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins". J. Virol. 65 (10): 4409–4416. PMID 2778882.
↑ Tombinson, S. and Taylor, P.W. (1985). "Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide". J. Virol. 55 (2): 374–378. PMID 3894684.
↑ Cabezas, J.A. (1991). "Some questions and suggestions on the type references of the official nomenclature (IUB) for sialidase(s) and endosialidase". Biochem. J. 278: 311–312. doi:10.1042/bj2780311. PMC 1151486. PMID 1883340.

External links

Endo-alpha-sialidase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases

Disaccharidase	Sucrase/Sucrase-isomaltase/Invertase Maltase Trehalase Lactase

Glucosidases	Cellulase Alpha-glucosidase Acid Neutral AB Neutral C Beta-glucosidase cytosolic Debranching enzyme

Other	Amylase Alpha-amylase Chitinase Lysozyme Neuraminidase NEU1 NEU2 NEU3 NEU4 Bacterial neuraminidase Viral neuraminidase Galactosidases Alpha Beta alpha-Mannosidase Glucuronidase Hyaluronidase Pullulanase Glucosylceramidase lysosomal non-lysosomal Galactosylceramidase Alpha-N-acetylgalactosaminidase NAGA Alpha-N-acetylglucosaminidase Fucosidase Hexosaminidase HEXA HEXB Iduronidase Maltase-glucoamylase Heparanase HPSE2

3.2.2: Hydrolysing
N-Glycosyl compounds

DNA glycosylases: Oxoguanine glycosylase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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