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Literature summary for 3.2.1.39 extracted from
- Structural and thermodynamic characterization of endo-1,3-beta-glucanase Insights into the substrate recognition mechanism (2018), Biochim. Biophys. Acta, 1866, 415-425 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Cellulosimicrobium cellulans |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in complex with laminarihexaose, single wavelength anomalous dispersion method, using a Na2AuCl4 derivative | Cellulosimicrobium cellulans |
| to 1.66 A resolution, and modeling of laminarihexaose into the substrate-binding cleft. The substrates bind to the subsites -1 to -3 with the highest affinity, while the part bound to the reducing end will be hydrolyzed. Comparison of the endo-1,3-beta-glucanase catalytic domain with other known GH16 enzyme structures | Cellulosimicrobium cellulans |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E119A | inactive | Cellulosimicrobium cellulans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cellulosimicrobium cellulans | G1ED17 | - |
- |
| Cellulosimicrobium cellulans DK-1 | G1ED17 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Cellulosimicrobium cellulans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| laminarihexaose + H2O | - |
Cellulosimicrobium cellulans | ? | - |
? |  |
| laminarihexaose + H2O | - |
Cellulosimicrobium cellulans DK-1 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| endo-beta-1,3-glucanase | - |
Cellulosimicrobium cellulans |
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Release 2023.1 (January 2023)
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