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Literature summary for 3.2.1.8 extracted from
- Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8 (2005), Proteins, 61, 999-1009.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in complex with xylotriose and xylobiose | Thermotoga maritima |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermotoga maritima | - |
- |
- |
| Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme folds into a (beta/alpha)8-barrel structure, and has characteristic clusters of aromatic residues together with a lack of exposed hydrophobic residues, crystallization data | Thermotoga maritima |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| TmxB | - |
Thermotoga maritima |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
features that account for the high thermostability of enzyme are clusters of aromatic residues together with a lack of exposed hydrophobic residues | Thermotoga maritima |
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Release 2023.1 (January 2023)
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