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Literature summary for 3.2.1.91 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
Search for more literature for 3.2.1.91

Cloned(Commentary)

Cloned (Comment) Organism
-
 Trichoderma reesei

Protein Variants

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

Organism

Organism UniProt Comment Textmining
Trichoderma reesei P07987
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Trichoderma reesei

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
Cel6A
-
 Trichoderma reesei

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Trichoderma reesei

pH Range

pH Minimum pH Maximum Comment Organism
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

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