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Literature summary for 3.2.1.129 extracted from

  • Schwarzer, D.; Browning, C.; Stummeyer, K.; Oberbeck, A.; Muehlenhoff, M.; Gerardy-Schahn, R.; Leiman, P.G.
    Structure and biochemical characterization of bacteriophage phi92 endosialidase (2015), Virology, 477, 133-143.
    View publication on PubMed
Search for more literature for 3.2.1.129

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-Gold(DE3) cells Enterobacteria phage phi92

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with a dimer of alpha-2,9-linked sialic acid, hanging drop vapor diffusion method, using 6% (w/v) PEG3350, 70 mM CHES buffer, pH 9.5 and 70 mM SrCl2 Enterobacteria phage phi92

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
capsular polysaccharides + H2O Enterobacteria phage phi92
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Enterobacteria phage phi92 I7HXG2
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-

Purification (Commentary)

Purification (Comment) Organism
HiTrap Q HP anion exchange column chromatography and Superdex 200 gel filtration Enterobacteria phage phi92

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
capsular polysaccharides + H2O
-
 Enterobacteria phage phi92 ?
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 ?
additional information the endosialidase is a bifunctional enzyme with high activity against alpha-2,8- and low activity against alpha-2,9-linkages in a polySia chain Enterobacteria phage phi92 ?
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 ?

Synonyms

Synonyms Comment Organism
endoN92 catalytic fragment Enterobacteria phage phi92
endosialidase
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 Enterobacteria phage phi92