EC Number | Application | Comment | Organism |
---|---|---|---|
4.1.3.3 | biotechnology | coupled bioconversion for preparation of N-acetyl-D-neuraminic acid using immobilized N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid lyase, a two-step enzymatic system involving immobilized both enzymes is used for the conversion of GlcNAc to NeuAc in a single reactor, optimum ratio is 3-6.25 U/ml of N-acetyl-D-glucosamine-2-epimerase and 12.5-25 U/ml of N-acetyl-D-neuraminic acid lyase | Sus scrofa |
5.1.3.8 | biotechnology | coupled bioconversion for preparation of N-acetyl-D-neuraminic acid using immobilized N-acetyl-D-glucosamine-2-epimerase and N-acetyl-D-neuraminic acid lyase, a two-step enzymatic system involving immobilized both enzymes is used for the conversion of GlcNAc to NeuAc in a single reactor, optimum ratio is 3-6.25 U/ml of N-acetyl-D-glucosamine-2-epimerase and 12.5-25 U/ml of N-acetyl-D-neuraminic acid lyase | Sus scrofa |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.3.3 | expressed in Escherichia coli BL21(DE3) cells | Escherichia coli |
4.1.3.3 | expression in Escherichia coli | Sus scrofa |
5.1.3.8 | expression in Escherichia coli | Sus scrofa |
EC Number | General Stability | Organism |
---|---|---|
4.1.3.3 | Amberzyme oxirane resin-immobilized NAL can be used up to five reaction cycles without loss of activity or significant decrease of the conversion rate, the activity yield of immobilized NAL is approximately 10% of the free enzyme | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.3.3 | N-acetyl-D-neuraminic acid | Sus scrofa | - |
N-acetyl-D-mannosamine + pyruvate | - |
r | |
5.1.3.8 | N-acetyl-D-mannosamine | Sus scrofa | - |
N-acetyl-D-glucosamine | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.3.3 | Escherichia coli | - |
- |
- |
4.1.3.3 | Escherichia coli TG1 | - |
- |
- |
4.1.3.3 | Sus scrofa | Q9BEC7 | - |
- |
5.1.3.8 | Sus scrofa | P17560 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.3.3 | by FP-based affinity chromatography | Sus scrofa |
4.1.3.3 | FPIDA-Co affinity support column chromatography | Escherichia coli |
5.1.3.8 | by FP-based affinity chromatography | Sus scrofa |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.1.3.3 | kidney | - |
Sus scrofa | - |
5.1.3.8 | kidney | - |
Sus scrofa | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.1.3.3 | additional information | - |
cell density of Escherichia coli BL21 (DE3) carrying the pNA1 plasmid is 37 (OD600) after fermentation for 15 h, and the highest activity for N-acetyl-D-neuraminic acid lyase is 8.472 U/ml after fermentation for 9 h, enzyme activity is assayed in reaction solution (20 mM Neu5Ac in 50 mM potassium phosphate buffer, pH 7.5) | Sus scrofa |
4.1.3.3 | 0.0693 | - |
immobilized recombinant enzyme, the activity yield of immobilized enzyme is approximately 10% of the free enzyme | Sus scrofa |
4.1.3.3 | 2.45 | - |
crude extract, in 50 mM potassium phosphate buffer, pH 7.5, at 37°C | Escherichia coli |
4.1.3.3 | 36.26 | - |
after 14.8fold purification, in 50 mM potassium phosphate buffer, pH 7.5, at 37°C | Escherichia coli |
4.1.3.3 | 36.26 | - |
purified enzyme after expression in Escherichia coli cells, enzyme activity is assayed in reaction solution (20 mM N-acetyl-D-neuraminic acid in 50 mM potassium phosphate buffer, pH 7.5) | Sus scrofa |
5.1.3.8 | additional information | - |
Escherichia coli cells harboring the recombinant plasmid are grown at 37°C in TB medium and induced by adding lactose to a final concentration of 1% lactose, samples are taken every 2 h, and the highest activity is 0.825 U/ml after fermentation for 22 h, activity is determined in 1 ml of reaction solution (100 mM Tris-HCl, pH 7.5, 100 mM GlcNAc, 10 mM MgCl2, and 2.5 mM ATP) | Sus scrofa |
5.1.3.8 | 0.07818 | - |
AGE, immobilized recombinant enzyme, the activity yield of immobilized enzyme is approximately 30% of the free enzyme, activity is determined in 1 ml of reaction solution (100 mM Tris-HCl, pH 7.5, 100 mM GlcNAc, 10 mM MgCl2, and 2.5 mM ATP) | Sus scrofa |
5.1.3.8 | 0.49 | - |
specific activity in crude extract after expression in Escherichia coli cells, activity is determined in 1 ml of reaction solution (100 mM Tris-HCl, pH 7.5, 100 mM GlcNAc, 10 mM MgCl2, and 2.5 mM ATP) | Sus scrofa |
5.1.3.8 | 29.13 | - |
recombinant enzyme after purification, activity is determined in 1 ml of reaction solution (100 mM Tris-HCl, pH 7.5, 100 mM GlcNAc, 10 mM MgCl2, and 2.5 mM ATP) | Sus scrofa |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.3.3 | N-acetyl-D-neuraminic acid | - |
Sus scrofa | N-acetyl-D-mannosamine + pyruvate | - |
r | |
4.1.3.3 | N-acetylneuraminate | - |
Escherichia coli | N-acetyl-D-mannosamine + pyruvate | - |
r | |
4.1.3.3 | N-acetylneuraminate | - |
Escherichia coli TG1 | N-acetyl-D-mannosamine + pyruvate | - |
r | |
5.1.3.8 | N-acetyl-D-mannosamine | - |
Sus scrofa | N-acetyl-D-glucosamine | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.3.3 | N-acetyl-D-neuraminic acid lyase | - |
Escherichia coli |
4.1.3.3 | N-acetyl-D-neuraminic acid lyase | - |
Sus scrofa |
4.1.3.3 | NAL | - |
Escherichia coli |
4.1.3.3 | NAL | - |
Sus scrofa |
5.1.3.8 | AGE | - |
Sus scrofa |
5.1.3.8 | N-acetyl-D-glucosamine-2-epimerase | - |
Sus scrofa |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.3.3 | 37 | - |
assay at | Sus scrofa |
5.1.3.8 | 37 | - |
assay at | Sus scrofa |