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Literature summary extracted from
- The thermophilic esterase from Archaeoglobus fulgidus: Structure and conformational dynamics at high temperature (2000), Proteins Struct. Funct. Genet., 38, 351-360.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.1 | Archaeoglobus fulgidus | O28558 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.1 | - |
Archaeoglobus fulgidus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.1 | AFEST | - |
Archaeoglobus fulgidus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | 80 | - |
- |
Archaeoglobus fulgidus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.1 | additional information | - |
between 20°C and 60°C a small but significant decrease of the beta-sheet bands occurrs, indicating a partial loss of beta-sheets. This suggests the presence of a temperature-sensitive beta-sheet. The increase in temperature from 60°C to 98°C induces a decrease of alpha-helix and beta-sheet bands which are still detected at 98°C indicating that at this temperature some secondary structure elements of the protein remain intact. The conformational dynamics of the esterase investigated by frequency-domain fluorometry and anisotropy decays show that the temperature affects the protein conformational dynamics | Archaeoglobus fulgidus |
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Release 2023.1 (January 2023)
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