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Literature summary for 1.14.99.53 extracted from
- Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus (2021), J. Biol. Chem., 297, 101084.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cellvibrio japonicus | B3PJ79 | - |
- |
| Cellvibrio japonicus Ueda107 | B3PJ79 | - |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | enzyme has two carbohydrate-binding modules, CBM5 and CBM73. Both CBMs bind crystalline chitin with Kd values in the micromolar range, CBM73 has higher affinity for chitin than CjCBM5. CBM5 binds soluble chitohexaose, whereas no binding of CBM73 chitohexaose is detected. In CBM5, conserved aromatic amino acids involved in substrate binding residues show a linear arrangement that seems compatible with the experimentally observed affinity for single chitin chains. The arrangement of these residues in CBM73 suggests a wider binding surface that may interact with several chitin chains | Cellvibrio japonicus |
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