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Literature summary for 1.1.3.4 extracted from
- Cloning and heterologous expression of glucose oxidase gene from Aspergillus niger Z-25 in Pichia pastoris (2010), Appl. Biochem. Biotechnol., 162, 498-509.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Pichia pastoris strain SMD1168 | Aspergillus niger |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 16.95 | - |
beta-D-glucose | recombinant enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, at 35°C | Aspergillus niger |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 94000 | - |
SDS-PAGE | Aspergillus niger |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | P13006 | - |
- |
| Aspergillus niger Z-25 | P13006 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| ammonium sulfate precipitation | Aspergillus niger |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 153.5 | - |
recombinant enzyme after 3.34fold purification, at 35°C | Aspergillus niger |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| beta-D-glucose + O2 + H2O | - |
Aspergillus niger | D-glucono-1,5-lactone + H2O2 | - |
? | |
| beta-D-glucose + O2 + H2O | - |
Aspergillus niger Z-25 | D-glucono-1,5-lactone + H2O2 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-D-glucose: oxygen 1-oxidoreductase | - |
Aspergillus niger |
| GOD | - |
Aspergillus niger |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
Aspergillus niger |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 60 | the activity of recombinant GOD increases slightly at the reaction temperature ranging from 20-40°C, and then falls moderately till 60°C. The recombinant enzyme retains more than 90% of activity within 40°C. Over 30% of activity is lost at 50°C, whereas almost no activity is detected above 60°C | Aspergillus niger |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 484.3 | - |
beta-D-glucose | recombinant enzyme, in 0.1 M sodium phosphate buffer, pH 6.0, at 35°C | Aspergillus niger | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Aspergillus niger |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 8 | more than 88% of the maximum activity is observed between pH 4.0 and 8.0, outside this range the activity decreases dramatically | Aspergillus niger |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Aspergillus niger | |
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Release 2023.1 (January 2023)
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