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Literature summary for 3.2.1.176 extracted from

  • Boer, H.; Koivula, A.
    The relationship between thermal stability and pH optimum studied with wild-type and mutant Trichoderma reesei cellobiohydrolase Cel7A (2003), Eur. J. Biochem., 270, 841-848.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E217Q stability similar to wild-type enzyme, catalytically inactive Trichoderma reesei
E223S/A224H/L225V/T226A/D262G mutant has a more alkaline pH optimum, mutation destabilizes the protein fold at both acidic and alkaline pH Trichoderma reesei

General Stability

General Stability Organism
cellotetraose stabilizes the protein fold Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Trichoderma reesei
-
-
-
Trichoderma reesei ALKO2877
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutants Trichoderma reesei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl-beta-D-lactoside + H2O
-
Trichoderma reesei ?
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
-
Trichoderma reesei ALKO2877 ?
-
?

pH Stability

pH Stability pH Stability Maximum Comment Organism
3.5 5.6 optimal stability, gradual decrease in stability at more alkaline pH values Trichoderma reesei