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Literature summary for 2.7.1.178 extracted from
- Soluble expression of archaeal proteins in Escherichia coli by using fusion-partners (2008), Protein Expr. Purif., 62, 116-119.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| produced as inclusion bodies in Escherichia coli when polyhistidine is used as a fusion tag. To reduce inclusion body formation in Escherichia coli, the enzyme is fused with three partners, thioredoxin, glutathione-S-transferase, and N-utilization substance A. With the use of fusion-partners, the solubility of the archaeal protein is remarkably enhanced, and the soluble fraction of the recombinant protein is increased in this order: thioredoxin > glutathione-S-transferase > N-utilization substance A. In the case of recombinant enzyme, the enzyme activity of the Trx-fused protein is 200-fold higher than that of the polyhistidine-fusion protein | Saccharolobus solfataricus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | Q97U29 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 2-keto-3-deoxy-D-gluconate kinase | - |
Saccharolobus solfataricus |
| KDGK | - |
Saccharolobus solfataricus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
assay at | Saccharolobus solfataricus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Saccharolobus solfataricus |
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Release 2023.1 (January 2023)
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