Organic Solvent | Comment | Organism |
---|---|---|
guanidine-HCl | 4.0-6.0 M, 1 h, complete denaturation. SsAspAT is fully unfolded in the presence of denaturant concentrations higher than 3.5 M | Saccharolobus solfataricus |
guanidine-HCl | at 25°C, the enzyme from Sulfolobus solfataricus is less resistant to guanidinium chloride-induced denaturation than the cytosolic mesophilic aspartate aminotransferase from pig heart | Saccharolobus solfataricus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | - |
- |
- |
Saccharolobus solfataricus | P14909 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharolobus solfataricus |
recombinant protein | Saccharolobus solfataricus |
Renatured (Comment) | Organism |
---|---|
refolding of SsAspAT can be accelerated by increasing the temperature from 25 to 50°C. Although refolding is faster at 50°C (35% of native enzyme) the highest yield of renaturation is obtained at 37°C (70% reactivation), similar to the yield of 65% of initial activity that is obtained at 25°C | Saccharolobus solfataricus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-cysteine sulfinic acid + 2-oxoglutarate | - |
Saccharolobus solfataricus | 2-oxo-3-sulfinopropionic acid + L-glutamate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Saccharolobus solfataricus |
Synonyms | Comment | Organism |
---|---|---|
aspartate aminotransferase | - |
Saccharolobus solfataricus |
SsAspAT | - |
Saccharolobus solfataricus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
100 | - |
- |
Saccharolobus solfataricus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
structural stability of the enzyme is investigated by coupling isothermally and thermally induced denaturation studies to molecular modeling. Gel filtration analysis indicates that the enzyme unfolds with an N2 reversible 2D mechanism. In the molecular model, a cluster of hydrophobic residues is shown at the interface between the subunits of the enzyme and suggests this cluster as a structural feature stabilizing the enzyme quaternary structure | Saccharolobus solfataricus |
100 | - |
the enzyme retains its structure at 100°C | Saccharolobus solfataricus |