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Literature summary for 3.2.1.129 extracted from

  • Jakobsson, E.; Jokilammi, A.; Aalto, J.; Ollikka, P.; Lehtonen, J.V.; Hirvonen, H.; Finne, J.
    Identification of amino acid residues at the active site of endosialidase that dissociate the polysialic acid binding and cleaving activities in Escherichia coli K1 bacteriophages (2007), Biochem. J., 405, 465-472.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Vectrevirus K1E
mutant proteins harbouring single amino acid substitutions expressed as GFP-fusion proteins Enterobacteria phage K1A

Protein Variants

Protein Variants Comment Organism
D489N back-mutations, partial reduction of enzymic activity. Single amino acid substitution do not inactivate the catalytic activity totally Enterobacteria phage K1A
H332N/N489D complete inactivation Enterobacteria phage K1A
H417Y/N489D complete inactivation Enterobacteria phage K1A
additional information N-terminal deletion mutants are catalytically active, whereas all C-terminally truncated mutants are inactive Enterobacteria phage K1A
additional information point mutation located on or near the putative active site, exhibits greatly reduced activity Vectrevirus K1E
R614G displays full endosialidase activity Vectrevirus K1E
R614G displays full endosialidase activity Enterobacteria phage K1A
Y417H back-mutations, partial reduction of enzymic activity. Single amino acid substitution do not inactivate the catalytic activity totally Enterobacteria phage K1A

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
76000
-
-
Enterobacteria phage K1A
89000
-
sequence analysis Enterobacteria phage K1A

Organism

Organism UniProt Comment Textmining
Enterobacteria phage K1A A4UUQ0
-
-
Vectrevirus K1E
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly(sialic) acid + H2O
-
Vectrevirus K1E ?
-
?
poly(sialic) acid + H2O
-
Enterobacteria phage K1A ?
-
?

Subunits

Subunits Comment Organism
monomer
-
Enterobacteria phage K1A

Synonyms

Synonyms Comment Organism
endo-N-acetylneuraminidase
-
Vectrevirus K1E
endo-N-acetylneuraminidase
-
Enterobacteria phage K1A
endosialidase
-
Vectrevirus K1E
endosialidase
-
Enterobacteria phage K1A