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Literature summary extracted from

  • Zhou, C.; Chen, X.; Feng, J.; Xiao, D.; Wu, Q.; Zhu, D.
    Molecular cloning and characterization of a N-acetylneuraminate lyase gene from Staphylococcus hominis (2013), Chin. J. Biotechnol., 29, 480-489.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.3.3 cloning and recombinant expression in Escherichia coli strain BL21(DE3) Staphylococcus hominis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.3.3 4
-
N-acetylneuraminate recombinant enzyme, pH and temperature not specified in the publication Staphylococcus hominis
4.1.3.3 35.1
-
pyruvate recombinant enzyme, pH and temperature not specified in the publication Staphylococcus hominis
4.1.3.3 131.7
-
N-acetyl-D-mannosamine recombinant enzyme, pH and temperature not specified in the publication Staphylococcus hominis

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.3 Staphylococcus hominis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.3 recombinant enzyme from Escherichia coli strain BL21(DE3) Staphylococcus hominis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.3 N-acetylneuraminate
-
Staphylococcus hominis N-acetyl-D-mannosamine + pyruvate
-
r

Subunits

EC Number Subunits Comment Organism
4.1.3.3 homotetramer recombinant enzyme Staphylococcus hominis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.3.3 45
-
syntesis reaction Staphylococcus hominis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.3.3 45
-
purified recombinant enzyme, 2 h, stable Staphylococcus hominis
4.1.3.3 50
-
above, purified recombinant enzyme, rapid decrease of activity Staphylococcus hominis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.3.3 7.5
-
synthesis reaction Staphylococcus hominis
4.1.3.3 8
-
cleavage reaction Staphylococcus hominis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.1.3.3 5 10 purified recombinant enzyme, 24 h, 4°C, different buffers, over 70% activity remains Staphylococcus hominis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.3.3 0.08
-
pyruvate recombinant enzyme, pH and temperature not specified in the publication Staphylococcus hominis
4.1.3.3 0.08
-
N-acetyl-D-mannosamine recombinant enzyme, pH and temperature not specified in the publication Staphylococcus hominis
4.1.3.3 1.9
-
N-acetylneuraminate recombinant enzyme, pH and temperature not specified in the publication Staphylococcus hominis