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Literature summary for 3.2.1.14 extracted from
- A new type of plant chitinase containing LysM domains from a fern (Pteris ryukyuensis): roles of LysM domains in chitin binding and antifungal activity (2008), Glycobiology, 18, 414-423.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Pteris ryukyuensis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E247Q | no chitinase activity, no antifungal activity | Pteris ryukyuensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pteris ryukyuensis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pteris ryukyuensis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Pteris ryukyuensis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the LysM domains contribute significantly to the antifungal activity of PrChi-A through their binding activity to chitin in the cell wall of fungi | Pteris ryukyuensis | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| chitinase-A | - |
Pteris ryukyuensis |
| PrChi-A | - |
Pteris ryukyuensis |
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Release 2023.1 (January 2023)
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