Endo-α-sialidase (EC 3.2.1.129, endo-N-acylneuraminidase, endoneuraminidase, endo-N-acetylneuraminidase, poly(α-2,8-sialosyl) endo-N-acetylneuraminidase, poly(α-2,8-sialoside) α-2,8-sialosylhydrolase, endosialidase, endo-N) is an enzyme with systematic namepolysialoside (2→8)-α-sialosylhydrolase.[1][2][3][4][5][6][7] It catalyses the following chemical reaction:
Endohydrolysis of (2→8)-α-sialosyl linkages in oligo- or poly(sialic) acids
Referencesedit
^Finne J, Mäkelä PH (January 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". The Journal of Biological Chemistry. 260 (2): 1265–70. doi:10.1016/S0021-9258(20)71238-X. PMID 3968060.
^Hallenbeck PC, Vimr ER, Yu F, Bassler B, Troy FA (March 1987). "Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-α-2,8-sialosyl carbohydrate units". The Journal of Biological Chemistry. 262 (8): 3553–61. doi:10.1016/S0021-9258(18)61387-0. PMID 3546309.
^Kitajima K, Inoue S, Inoue Y, Troy FA (December 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". The Journal of Biological Chemistry. 263 (34): 18269–76. doi:10.1016/S0021-9258(19)81355-8. PMID 3142874.
^Kwiatkowski B, Boschek B, Thiele H, Stirm S (August 1982). "Endo-N-acetylneuraminidase associated with bacteriophage particles". Journal of Virology. 43 (2): 697–704. doi:10.1128/JVI.43.2.697-704.1982. PMC256172. PMID 7109038.
^Pelkonen S, Pelkonen J, Finne J (October 1989). "Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins". Journal of Virology. 63 (10): 4409–16. doi:10.1128/JVI.63.10.4409-4416.1989. PMC251059. PMID 2778882.
^Tomlinson S, Taylor PW (August 1985). "Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide". Journal of Virology. 55 (2): 374–8. doi:10.1128/JVI.55.2.374-378.1985. PMC254943. PMID 3894684.
^Cabezas JA (August 1991). "Some questions and suggestions on the type references of the official nomenclature (IUB) for sialidase(s) and endosialidase". The Biochemical Journal. 278 ( Pt 1) (Pt 1): 311–2. doi:10.1042/bj2780311. PMC1151486. PMID 1883340.
endo, alpha, sialidase, endo, sialidase, endo, acylneuraminidase, endoneuraminidase, endo, acetylneuraminidase, poly, sialosyl, endo, acetylneuraminidase, poly, sialoside, sialosylhydrolase, endosialidase, endo, enzyme, with, systematic, name, polysialoside, s. Endo a sialidase EC 3 2 1 129 endo N acylneuraminidase endoneuraminidase endo N acetylneuraminidase poly a 2 8 sialosyl endo N acetylneuraminidase poly a 2 8 sialoside a 2 8 sialosylhydrolase endosialidase endo N is an enzyme with systematic name polysialoside 2 8 a sialosylhydrolase 1 2 3 4 5 6 7 It catalyses the following chemical reaction Endo a sialidaseIdentifiersEC no 3 2 1 129CAS no 91195 87 8DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins Endohydrolysis of 2 8 a sialosyl linkages in oligo or poly sialic acidsReferences edit Finne J Makela PH January 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 The Journal of Biological Chemistry 260 2 1265 70 doi 10 1016 S0021 9258 20 71238 X PMID 3968060 Hallenbeck PC Vimr ER Yu F Bassler B Troy FA March 1987 Purification and properties of a bacteriophage induced endo N acetylneuraminidase specific for poly a 2 8 sialosyl carbohydrate units The Journal of Biological Chemistry 262 8 3553 61 doi 10 1016 S0021 9258 18 61387 0 PMID 3546309 Kitajima K Inoue S Inoue Y Troy FA December 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 The Journal of Biological Chemistry 263 34 18269 76 doi 10 1016 S0021 9258 19 81355 8 PMID 3142874 Kwiatkowski B Boschek B Thiele H Stirm S August 1982 Endo N acetylneuraminidase associated with bacteriophage particles Journal of Virology 43 2 697 704 doi 10 1128 JVI 43 2 697 704 1982 PMC 256172 PMID 7109038 Pelkonen S Pelkonen J Finne J October 1989 Common cleavage pattern of polysialic acid by bacteriophage endosialidases of different properties and origins Journal of Virology 63 10 4409 16 doi 10 1128 JVI 63 10 4409 4416 1989 PMC 251059 PMID 2778882 Tomlinson S Taylor PW August 1985 Neuraminidase associated with coliphage E that specifically depolymerizes the Escherichia coli K1 capsular polysaccharide Journal of Virology 55 2 374 8 doi 10 1128 JVI 55 2 374 378 1985 PMC 254943 PMID 3894684 Cabezas JA August 1991 Some questions and suggestions on the type references of the official nomenclature IUB for sialidase s and endosialidase The Biochemical Journal 278 Pt 1 Pt 1 311 2 doi 10 1042 bj2780311 PMC 1151486 PMID 1883340 External links editEndo alpha sialidase at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology nbsp This enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Endo alpha sialidase amp oldid 1172345674, wikipedia, wiki, book, books, library,
