Endo-alpha-sialidase (EC3.2.1.129, 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 namepolysialoside (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. PMID3968060.
^Hallenbeck, P.C.; Vimr, E.R.; Yu, F.; Bassler, B.; 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. PMID3546309.
^Kitakima, K.; Inoue, S.; Inoue, Y.; 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. PMID3142874.
^Kwiatkowski, B.; Boscheck, B.; Thicle, H.; Stirm, S. (1982). "Endo-N-acetylneuraminidase associated with bacteriophage particles". J. Virol. 43 (2): 697–704. PMID7109038.
^Pelkonen, S.; Pelkonen, J.; Finne, J. (1989). "Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins". J. Virol. 65 (10): 4409–4416. PMID2778882.
^Tombinson, S.; Taylor, P.W. (1985). "Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide". J. Virol. 55 (2): 374–378. PMID3894684.
