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Literature summary extracted from
- Kinetic study of the thermal denaturation of a hyperthermostable extracellular alpha-amylase from Pyrococcus furiosus (2013), Biochim. Biophys. Acta, 1834, 2600-2605.
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.1 | extracellular | - |
Pyrococcus furiosus | - |
- |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | Pyrococcus furiosus | - |
- |
- |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 106 | - |
denaturation of the enzyme is irreversible above a Tm of approximately 106°C and can be described by a one-step irreversible model | Pyrococcus furiosus |
| 3.2.1.1 | 117 | - |
t1/2: 10.1 min | Pyrococcus furiosus |
| 3.2.1.1 | 121 | - |
t1/2: 6.1 min, activation energy at 121°C is 316kJ/mol. Under an isothermal holding temperature of 121°C, the structure of the enzyme changes during denaturation from an alpha-helical structure, through a beta-sheet structure to an aggregated protein | Pyrococcus furiosus |
| 3.2.1.1 | 125 | - |
t1/2: 2.7 min | Pyrococcus furiosus |
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