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Literature summary for 3.1.31.1 extracted from
- Local stability identification and the role of a key aromatic amino acid residue in staphylococcal nuclease refolding (2005), FEBS J., 272, 3960-3966.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| DELTA1-139 | mutant lacks tertiary structure, fluorescence of the mutant is much lower than that of the wild-type enzyme | Staphylococcus sp. |
| DELTA1-141 | intact tertiary conformation, melting point is nearly identical to wild-type enzyme | Staphylococcus sp. |
| K133A | intact tertiary conformation, melting point is 4.6°C lower than that of the wild-type enzyme | Staphylococcus sp. |
| W140A | mutant lacks tertiary structure, fluorescence of the mutant is much lower than that of the wild-type enzyme | Staphylococcus sp. |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus sp. | - |
recombinant | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Staphylococcus sp. |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SNase | - |
Staphylococcus sp. |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 48 | - |
melting point of mutant enzyme K133A is 47.7°C | Staphylococcus sp. |
| 52 | - |
melting poit of the wild-type enzyme is 52.32° | Staphylococcus sp. |
| 53 | - |
melting point of the mutant enzyme DELTA1-141 is 52.8°C | Staphylococcus sp. |
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