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Literature summary for 1.4.3.21 extracted from
- Osmolytic effect of sucrose on thermal denaturation of pea seedling copper amine oxidase (2017), Protein J., 36, 147-153 .
General Stability
| General Stability | Organism |
|---|---|
| sucrose stabilizes the enzyme in terms of activity, secondary and tertiary structure. On the other hand sucrose reduces unfolding rate constant at given temperature. These effects can be the result of strengthening the water cage around the protein which limits oscillation frequency of the protein during unfolding process | Pisum sativum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pisum sativum | Q43077 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pisum sativum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| seedling | - |
Pisum sativum | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| putrescine + H2O + O2 | - |
Pisum sativum | 4-aminobutanal + NH3 + H2O2 | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PSAO | - |
Pisum sativum |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 63 | - |
when incubated at 63 °C the enzyme loses more than 90% of its activity in the first hour while in presence of 1 M sucrose, its inactivation appears after 10 min incubation at 70°C | Pisum sativum |
| 70 | - |
when incubated at 63 °C the enzyme loses more than 90% of its activity in the first hour while in presence of 1 M sucrose, its inactivation appears after 10 min incubation at 70°C | Pisum sativum |
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Release 2023.1 (January 2023)
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