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Literature summary for 3.2.1.18 extracted from

  • Johansson, B.E.; Brett, I.C.
    Variation in the divalent cation requirements of influenza A virus N2 neuraminidases (2003), J. Biochem., 134, 345-352.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
influenza A virus
Zn2+ slight inhibition influenza A virus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics influenza A virus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates about 2fold, increase in initial reaction velocity, required influenza A virus
Mg2+ activates about 2fold, increase in initial reaction velocity, required influenza A virus
additional information decrease in activity through removal of divalent cations results in decreased immunogenicity, antibody response decreases by about 68-76%, 80% of the original activity is restored by addition of Ca2+ and Mg2+ influenza A virus

Organism

Organism UniProt Comment Textmining
influenza A virus
-
type N2, several strains
-

Purification (Commentary)

Purification (Comment) Organism
from several strains influenza A virus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
activity of different strains in presence or absence of divalent cations, overview influenza A virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid + H2O
-
influenza A virus 4-methylumbelliferol + alpha-D-N-acetylneuraminic acid
-
?

Synonyms

Synonyms Comment Organism
NA
-
influenza A virus
neuraminidase
-
influenza A virus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at influenza A virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.9
-
assay at influenza A virus