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Literature summary for 3.2.1.58 extracted from
- Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in Candida albicans adhesion by the human antimicrobial peptide LL-37 (2011), PLoS ONE, 6, e21394.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| LL-37 | antimicrobial peptide derived from human cathelicidin, by proteinase-3 cleavage. LL-37 significantly reduces Candida albicans adhesion to plastic, oral epidermoid OECM-1 cells, and urinary bladders of female BALB/c mice. LL-37 reduces Xog1 activity and thus interrupts cell-wall remodeling | Candida albicans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Candida albicans | P29717 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Xog1 | - |
Candida albicans |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | deletion of XOG1 leads to decrease in cellular exoglucanase activity, cell adhesion and binding of antimicrobial peptide LL-37. Antibodies against Xog1p also decrease cell adhesion. Xog1 has a role in Candida albicans adhesion to polystyrene and, by inference, attachment to host cells via direct or indirect manners | Candida albicans |
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