Any feedback?
Literature summary for 3.2.1.91 extracted from
- Hydrolysis of microcrystalline cellulose by cellobiohydrolase I and endoglucanase II from Trichoderma reesei Adsorption, sugar production pattern, and synergism of the enzymes (1998), Biotechnol. Bioeng., 59, 621-634 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trichoderma reesei | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Trichoderma reesei |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| avicel + H2O | cellobiohydrolase I when acting on Avicel, is not perfectly processive, the cellulose chain is released from the active site after 5-10 cellobiose units have been cleaved off. Adsorption of endoglucanase II and cellobiohydrolase I iss mutually negatively affected by the presence of the other enzyme. This can be the result of (i) depletion (hydrolysis) of common binding sites or (ii) competition for (occupation of) common adsorption sites. Importance of competition is shown by the concentration dependence of the observed decrease in adsorption. Cellobiohydrolase I is competing more efficiently for the binding sites than endoglucanase II. Adsorption results indicate that, besides common adsorption sites (for which endoglucanase II and cellobiohydrolase I compete), the enzymes have specific sites as well | Trichoderma reesei | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CBH I | - |
Trichoderma reesei |
| cellobiohydrolase I | - |
Trichoderma reesei |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
