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Literature summary for 1.1.5.2 extracted from
- Engineering a chimeric pyrroloquinoline quinone glucose dehydrogenase: improvement of EDTA tolerance, thermal stability and substrate specificity (1999), Protein Eng., 12, 63-70.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | Escherichia coli |
| additional information | improved EDTA tolerance, thermal stability and substrate specificity of chimeric proteins | Acinetobacter calcoaceticus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the protein region responsible for complete EDTA tolerance is located between 32% and 59% from the N-terminus, A27 region | Acinetobacter calcoaceticus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acinetobacter calcoaceticus | - |
- |
- |
| Escherichia coli | - |
- |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the C-terminal 3% region, A3 region, plays an important role in the increase of thermal stability | Escherichia coli |
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Release 2023.1 (January 2023)
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