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Literature summary extracted from
- The role of phenylalanine 31 in maintaining the conformational stability of ribonuclease P2 from Sulfolobus solfataricus under extreme conditions of temperature and pressure. (1997), Biochemistry, 36, 8733-8742.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.6.1.18 | F31A | considerable decrease in stability against heat and pressure. Analysis of thermodynamic parameters | Saccharolobus solfataricus |
| 4.6.1.18 | F31Y | considerable decrease in stability against heat and pressure. Analysis of thermodynamic parameters | Saccharolobus solfataricus |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 4.6.1.18 | wild-type enzyme is extremely stable under all conditions of temperature and pressure applied. Thermodynamic analysis of heat and cold denaturation | Saccharolobus solfataricus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.6.1.18 | Saccharolobus solfataricus | P61991 | isoform P2 | - |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.6.1.18 | More | strong van der Waals interaction energy between residues F5, F31, and Y33 | Saccharolobus solfataricus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.6.1.18 | -20 | 90 | wild-type enzyme is extremely stable under all conditions of temperature and pressure applied. Thermodynamic analysis of heat and cold denaturation | Saccharolobus solfataricus |
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Release 2023.1 (January 2023)
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