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Literature summary for 3.2.1.B26 extracted from
- Temperature-induced denaturation of beta-glycosidase from the archaeon Sulfolobus solfataricus (1996), J. Biochem., 120, 292-300.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Saccharolobus solfataricus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 240000 | - |
- |
Saccharolobus solfataricus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | - |
- |
- |
| Saccharolobus solfataricus MT4 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharolobus solfataricus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | - |
Saccharolobus solfataricus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 95 | barely active at 30°C, optimal activity over 95°C | Saccharolobus solfataricus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
denaturation temperature. The temperature-induced denaturation of this tetrameric enzyme is a complex and irreversible process, in which subunit dissociation is coupled with unfolding, while unfolded polypeptide chains tend to associate in a nonspecific manner | Saccharolobus solfataricus |
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