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Literature summary extracted from
- Study of protein conformational stability and integrity using calorimetry and FT-Raman spectroscopy correlated with enzymatic activity (2008), Eur. J. Pharm. Sci., 33, 177-190.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.21.1 | additional information | thermal stress substantially perturbs the secondary structure of DNase I. Accordingly, heating of solid DNase I samples to temperatures below or above the apparent denaturation temperatures of the solid protein degrades and hence denatures the protein. For denatured DNase I samples, the residual biological activities after heating to 125°C are 37% and the activities after heating to 210°C are ca. 8%. Thermal denaturation of DNase I in high sensitivity differential scanning calorimetry is not reversible upon cooling of thermally denatured proteins (in contrast to lysozyme). Lyophilised lysozyme better refolds than spray-dried DNase I | Bos taurus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.21.1 | Bos taurus | - |
- |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 3.1.21.1 | Thermal denaturation of DNase I in high sensitivity differential scanning calorimetry is not reversible upon cooling of thermally denatured proteins (in contrast to lysozyme). Lyophilised lysozyme better refolds than spray-dried DNase I | Bos taurus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.21.1 | pancreas | - |
Bos taurus | - |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.21.1 | deoxyribonuclease I | - |
Bos taurus |
| 3.1.21.1 | DNase I | - |
Bos taurus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.21.1 | additional information | - |
thermal stress substantially perturbs the secondary structure of DNase I. Accordingly, heating of solid DNase I samples to temperatures below or above the apparent denaturation temperatures of the solid protein degrades and hence denatures the protein. For denatured DNase I samples, the residual biological activities after heating to 125°C are 37% and the activities after heating to 210°C are ca. 8% | Bos taurus |
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Release 2023.1 (January 2023)
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