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Literature summary for 3.2.1.176 extracted from

  • Wahlstroem, R.; Rahikainen, J.; Kruus, K.; Suurnaekki, A.
    Cellulose hydrolysis and binding with Trichoderma reesei Cel5A and Cel7A and their core domains in ionic liquid solutions (2014), Biotechnol. Bioeng., 111, 726-733.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,3-dimethylimidazolium dimethylphosphate complete inhibition at 30% v/v, ionic liquids inactivate cellulases, the enzyme is sensitive against 1,3-dimethylimidazolium dimethylphosphate and 1-ethyl-3-methylimidazolium acetate, effects on cellulase substrate binding, overview Trichoderma reesei
1-ethyl-3-methylimidazolium acetate complete inhibition at 30% v/v, ionic liquids inactivate cellulases, the enzyme is sensitive against 1,3-dimethylimidazolium dimethylphosphate and 1-ethyl-3-methylimidazolium acetate, effects on cellulase substrate binding, overview Trichoderma reesei

Organism

Organism UniProt Comment Textmining
Trichoderma reesei G0RVK1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl-beta-D-lactoside + H2O
-
Trichoderma reesei 4-methylumbelliferol + D-lactose
-
?
microcrystalline cellulose + H2O
-
Trichoderma reesei ?
-
?
additional information enzyme Cel7A hydrolyses the cellulose from the reducing chain end in a processive manner Trichoderma reesei ?
-
?

Synonyms

Synonyms Comment Organism
Cel7A
-
Trichoderma reesei
cellobiohydrolase
-
Trichoderma reesei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
assay at Trichoderma reesei

pH Optimum

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

General Information

General Information Comment Organism
additional information the core domain is able to bind tightly to cellulose, even in absence of the carbohydrate-binding module. Family 1 carbohydrate-binding modules are small wedge-shaped domains with a rough and a flat face. Carbohydrate-binding module interaction with crystalline cellulose surfaces takes place through three tyrosine residues aligned on the flat face forming hydrogen bonds with the cellulose substrate Trichoderma reesei