Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Trichoderma reesei |
Crystallization (Comment) | Organism |
---|---|
molecular dynamics simulation and data analysis protocol to identify the weak spots of Trichoderma reesei Cel7B, through assigning the local melting temperature to individual residue pairs. To test the predicted weak spots, a total of eight disulfide bonds are designed in these regions and all enhance the enzyme thermostability. The increased stability, is negatively correlated with the molecular dynamics-predicted melting temperature | Trichoderma reesei |
Protein Variants | Comment | Organism |
---|---|---|
G155C/G169C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 54.9°C, decrease in activity with filter paper and avicel | Trichoderma reesei |
G155C/N182C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.5°C, decrease in activity with filter paper and avicel | Trichoderma reesei |
G155C/N182C/N160C/G183C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.9°C, decrease in activity with filter paper | Trichoderma reesei |
G4C/E73C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.9°C, decrease in activity with filter paper and avicel | Trichoderma reesei |
G4C/F71C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.9°C, decrease in activity with avicel | Trichoderma reesei |
G4C/F71C/G155C/N182C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 60.7°C, increase in activity with filter paper and avicel | Trichoderma reesei |
G4C/F71C/G155C7N182C/N160C/G183C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 60.6°C, decrease in activity with filter paper and avicel | Trichoderma reesei |
G4C/F71C/N160C/G183C | introduction of disulfide bonds for stabilization of the catalytic domain, melting temperature 60.4°C, decrease in activity with filter paper and avicel | Trichoderma reesei |
G4C/F71C/N160C/G183C/S168T | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 62.8°C, increase in activity with filter paper and avicel | Trichoderma reesei |
G81C/V105C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 55.9°C, decrease in activity with filter paper and avicel | Trichoderma reesei |
N160C/G183C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 56.8°C, decrease in activity with filter paper and avicel | Trichoderma reesei |
S213C/A296C | introduction of disulfide bond for stabilization of the catalytic domain, melting temperature 55.3°C, decrease in activity with filter paper and avicel | Trichoderma reesei |
Y326C/G343C | introduction of disulfide bonds for stabilization of the catalytic domain, melting temperature 57.3°C, increase in activity with filter paper and decrease in activity with avicel | Trichoderma reesei |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Trichoderma reesei | G0RKH9 | - |
- |
Trichoderma reesei QM6a | G0RKH9 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
avicel + H2O | - |
Trichoderma reesei | ? | - |
? | |
avicel + H2O | - |
Trichoderma reesei QM6a | ? | - |
? | |
filter paper + H2O | - |
Trichoderma reesei | ? | - |
? | |
filter paper + H2O | - |
Trichoderma reesei QM6a | ? | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
54.6 | - |
wild-type catalytic domain, melting temperature | Trichoderma reesei |