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Literature summary for 3.4.21.63 extracted from
- Thermodynamic investigation of an alkaline protease from Aspergillus tamarii URM4634 a comparative approach between crude extract and purified enzyme (2018), Int. J. Biol. Macromol., 109, 1039-1044 .
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | thermodynamic and kinetic studies, simultaneous occurrence of a reversible equilibrium of enzyme unfolding, which is pushed to the right by a temperature increase, estimation of the activation energy of the hydrolysis reaction catalyzed by crude extract and purified protease as well as the respective standard enthalpy variations of reversible enzyme unfolding, overview | Aspergillus tamarii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus tamarii | - |
isolated from the soil of Caatinga, in Caninde de Sao Francisco, SE, Brazil | - |
| Aspergillus tamarii URM4634 | - |
isolated from the soil of Caatinga, in Caninde de Sao Francisco, SE, Brazil | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme by anion exchange chromatography | Aspergillus tamarii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| azocasein + H2O | - |
Aspergillus tamarii | ? | - |
? |  |
| azocasein + H2O | - |
Aspergillus tamarii URM4634 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Alkaline protease | - |
Aspergillus tamarii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 28 | - |
assay at | Aspergillus tamarii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 80 | when temperature is raised from 50°C to 80°C in activity assays, the specific rate constant of crude proteolytic extract thermoinactivation increases from 0.0072 to 0.0378 per min, while that of purified protease from 0.0099 to 0.0235 per min. These values, corresponding to half-life decreases from 96.3 to 18.3 min and from 70.0 to 29.5 min, respectively, allow to estimate the activation energy, enthalpy, entropy, and Gibbs free energy of thermoinactivation, overview | Aspergillus tamarii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Aspergillus tamarii |
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Release 2023.1 (January 2023)
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