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Literature summary for 6.3.1.2 extracted from
- Compatible solute effects on thermostability of glutamine synthetase and aspartate transcarbamoylase from Methanococcus jannaschii (2005), Biochim. Biophys. Acta, 1753, 164-173.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Methanocaldococcus jannaschii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanocaldococcus jannaschii | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Methanocaldococcus jannaschii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
- |
Methanocaldococcus jannaschii |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 70 | about 50% of maximal activity at 40°C and at 70°C | Methanocaldococcus jannaschii |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 57 | - |
midpoint temperature of pure enzyme, none of the small molecules tested significantly stabilizes the enzyme. Stabilization by Escherichia coli GroEL or ribosomal protein L2. Protein-protein interactions appear to be the dominant factor in stabilizing the archael enzyme at the growth temperature (85°C) | Methanocaldococcus jannaschii |
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Release 2023.1 (January 2023)
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