EC Number | Cloned (Comment) | Organism |
---|---|---|
2.5.1.56 | gene siaC, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta 2, subcloningin Escherichia coli strain DH5alpha | Idiomarina loihiensis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.56 | EDTA | slightly inhibitory at 1 mM | Idiomarina loihiensis | |
2.5.1.56 | K+ | 27% inhibition at 1 mM | Idiomarina loihiensis | |
2.5.1.56 | additional information | no or poor effect by Mg2+ and Ca2+ at 1 mM | Idiomarina loihiensis | |
2.5.1.56 | Na+ | slightly inhibitory at 1 mM | Idiomarina loihiensis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.5.1.56 | Co2+ | slightly activating at 1 mM | Idiomarina loihiensis | |
2.5.1.56 | Mn2+ | slightly activating at 1 mM | Idiomarina loihiensis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.5.1.56 | 41000 | - |
- |
Idiomarina loihiensis |
2.5.1.56 | 45000 | - |
- |
Idiomarina loihiensis |
2.5.1.56 | 95000 | - |
gel filtration | Idiomarina loihiensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.56 | phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O | Idiomarina loihiensis | - |
phosphate + N-acetylneuraminate | - |
ir | |
2.5.1.56 | phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O | Idiomarina loihiensis L2-TR | - |
phosphate + N-acetylneuraminate | - |
ir |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.56 | Idiomarina loihiensis | Q5R082 | gene siaC | - |
2.5.1.56 | Idiomarina loihiensis L2-TR | Q5R082 | gene siaC | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.5.1.56 | recombinant His-tagged enzyme from Escherichia coli strain Rosetta 2 by ultrafiltration, nickel affinity chromatography, and gel filtration | Idiomarina loihiensis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.56 | additional information | the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc | Idiomarina loihiensis | ? | - |
? | |
2.5.1.56 | additional information | the enzyme shows activity towards 2-acetamido-4-O-acetyl-2-deoxy-D-mannopyranose resulting in formation of 4-O-acetyl-ManNAc | Idiomarina loihiensis L2-TR | ? | - |
? | |
2.5.1.56 | phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O | - |
Idiomarina loihiensis | phosphate + N-acetylneuraminate | - |
ir | |
2.5.1.56 | phosphoenolpyruvate + N-acetyl-D-mannosamine + H2O | - |
Idiomarina loihiensis L2-TR | phosphate + N-acetylneuraminate | - |
ir |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.56 | homodimer | 2 * 45000, about, recombinant enzyme, SDS-PAGE, 2 * 41000, about, recombinant enzyme, HPLC/MS/ESI | Idiomarina loihiensis |
2.5.1.56 | More | the enzyme structure has a distinct domain architecture 4 without a cystathionine-beta-synthase domain (cystathionine-beta-synthetase domain), unlike domain architecture 3. The arginine essential for catalysis, that is present in antifreeze-like domain (block X), is not fully conserved in NeuB, but is replaced by a serine in domain architectures 3 and 4, three-dimensional structure comparison, and secondary structure element comparisons, detailed overview | Idiomarina loihiensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.56 | N-acetylneuraminate lyase synthase | - |
Idiomarina loihiensis |
2.5.1.56 | NeuB1 | - |
Idiomarina loihiensis |
2.5.1.56 | sialic acid synthase | UniProt | Idiomarina loihiensis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.5.1.56 | 40 | - |
- |
Idiomarina loihiensis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.5.1.56 | 40 | 60 | purified recombinant enzyme, pH 8.0, reasonably stable, maintaining 60% activity after 4 h at 40, and 50% activity after 30 min at 50°C, and almost fully inactivated at 60°C after 1 h | Idiomarina loihiensis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.5.1.56 | 7 | - |
- |
Idiomarina loihiensis |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
2.5.1.56 | 8 | - |
purified recombinant enzyme, 37°C, half-life is 8 h | Idiomarina loihiensis |
2.5.1.56 | 9 | - |
purified recombinant enzyme, 37°C, half-life is 2 h, inactivation after 4 h | Idiomarina loihiensis |
2.5.1.56 | 10 | - |
purified recombinant enzyme, 37°C, half-life is 1 h, inactivation after 3 h | Idiomarina loihiensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.5.1.56 | physiological function | key enzyme in microorganisms for producing N-acetylneuraminic acid through the irreversible condensation of N-acetylmannosamine and phosphoenolpyruvate | Idiomarina loihiensis |