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Literature summary extracted from

  • Wohlfahrt, G.; Pellikka, T.; Boer, H.; Teeri, T.T.; Koivula, A.
    Probing pH-dependent functional elements in proteins: modification of carboxylic acid pairs in Trichoderma reesei cellobiohydrolase Cel6A (2003), Biochemistry, 42, 10095-10103.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.91
-
Trichoderma reesei

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.91 E107Q mutant enzyme is destabilized at acidic pH and stabilized at alkaline pH Trichoderma reesei
3.2.1.91 E107Q/D170N/D366N mutant enzyme is destabilized at acidic pH and stabilized at alkaline pH Trichoderma reesei

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.91 Trichoderma reesei P07987
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.91
-
Trichoderma reesei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.91 cellotetraose + H2O
-
Trichoderma reesei cellobiose + D-glucose + cellotriose
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.91 Cel6A
-
Trichoderma reesei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.91 44
-
assay at Trichoderma reesei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.91 5
-
-
Trichoderma reesei

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.91 5 7 optimum at pH 5, drop of activity between pH 6 and pH 7 to about 30% of the maximal activity Trichoderma reesei

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.91 6
-
wild-type enzyme is more stable than E107Q and E107Q/D170N/D366N mutants Trichoderma reesei
3.2.1.91 8
-
wild-type enzyme is less stable than E107Q and E107Q/D170N/D366N mutants Trichoderma reesei