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Literature summary for 3.2.1.4 extracted from

  • Zhang, S.; Wang, Y.; Song, X.; Hong, J.; Zhang, Y.; Yao, L.
    Improving Trichoderma reesei Cel7B thermostability by targeting the weak spots (2014), J. Chem. Inf. Model., 54, 2826-2833.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Trichoderma reesei

Crystallization (Commentary)

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

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

Organism UniProt Comment Textmining
Trichoderma reesei G0RKH9
-
-
Trichoderma reesei QM6a G0RKH9
-
-

Substrates and Products (Substrate)

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 [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
54.6
-
wild-type catalytic domain, melting temperature Trichoderma reesei