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Literature summary for 2.5.1.56 extracted from

  • Suryanti, V.; Nelson, A.; Berry, A.
    Cloning, over-expression, purification, and characterization of N-acetylneuraminate synthase from Streptococcus agalactiae (2003), Protein Expr. Purif., 27, 346-356.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Streptococcus agalactiae

General Stability

General Stability Organism
expression of the native neuB gene product enzyme in E. coli results in a product that is prone to proteolysis during purification so the protein is tagged with a hexa-histidine tag at its N-terminus and rapidly purified Streptococcus agalactiae

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ 10 mM CuCl2, 90% inhibition Streptococcus agalactiae
EDTA 1 or 10 mM, 97% inhibition Streptococcus agalactiae
Fe2+ 1 mM FeCl2, 40% inhibition Streptococcus agalactiae
K+ 1 mM KCl, 92% inhibition Streptococcus agalactiae
Li+ 1 mM LiCl, 30% inhibition Streptococcus agalactiae
Na+ 1 mM NaCl, 20% inhibition Streptococcus agalactiae
Phenylglyoxal N-acetylmannosamine or phosphoenolpyruvate protect Streptococcus agalactiae
Zn2+ 1 mM ZnCl2, 80% inhibition Streptococcus agalactiae

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 1 mM stimulates around 2fold, the enzyme is dependent on the presence of metal ions such as Mg2+, Mn2+ or Co2+ Streptococcus agalactiae
Mg2+ the enzyme is dependent on the presence of metal ions such as Mg2+, Mn2+ or Co2+ Streptococcus agalactiae
Mn2+ 1 mM stimulates around 2fold, the enzyme is dependent on the presence of metal ions such as Mg2+, Mn2+ or Co2+ Streptococcus agalactiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38987
-
2 * 38987, electrospray ionisation mass spectrometry Streptococcus agalactiae
78000
-
gel filtration Streptococcus agalactiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O Streptococcus agalactiae the enzyme is involved in sialic acid synthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Streptococcus agalactiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
expression of the native neuB gene product enzyme in E. coli results in a product that is prone to proteolysis during purification so the protein is tagged with a hexa-histidine tag at its N-terminus and rapidly purified Streptococcus agalactiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information arginine residues are present in the active site and are involved in substrate recognition and binding Streptococcus agalactiae ?
-
?
N-acetyl-D-galactosamine + phosphoenolpyruvate + H2O 15% of the activity with N-acetyl-D-mannosamine Streptococcus agalactiae ?
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O
-
Streptococcus agalactiae N-acetylneuraminate + phosphate
-
?
N-acetyl-D-mannosamine + phosphoenolpyruvate + H2O the enzyme is involved in sialic acid synthesis Streptococcus agalactiae ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 38987, electrospray ionisation mass spectrometry Streptococcus agalactiae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
thermostable up to Streptococcus agalactiae
50
-
30 min, 80-90% loss of activity Streptococcus agalactiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Streptococcus agalactiae