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Literature summary 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)

EC Number Cloned (Comment) Organism
2.5.1.56 overexpression in Escherichia coli Streptococcus agalactiae

General Stability

EC Number General Stability Organism
2.5.1.56 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

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.5.1.56 Co2+ 1 mM stimulates around 2fold, the enzyme is dependent on the presence of metal ions such as Mg2+, Mn2+ or Co2+ Streptococcus agalactiae
2.5.1.56 Mg2+ the enzyme is dependent on the presence of metal ions such as Mg2+, Mn2+ or Co2+ Streptococcus agalactiae
2.5.1.56 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.5.1.56 38987
-
 2 * 38987, electrospray ionisation mass spectrometry Streptococcus agalactiae
2.5.1.56 78000
-
 gel filtration Streptococcus agalactiae

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.56 Streptococcus agalactiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.56 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)

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

Subunits

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.5.1.56 37
-
 thermostable up to Streptococcus agalactiae
2.5.1.56 50
-
 30 min, 80-90% loss of activity Streptococcus agalactiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.5.1.56 7
-
-
 Streptococcus agalactiae