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Literature summary for 3.4.13.22 extracted from
- Biochemical and biophysical characterization of an unexpected bacteriolytic activity of VanX, a member of the vancomycin-resistance vanA gene cluster (2014), J. Biol. Chem., 289, 35686-35694.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | strong bacteriolysis occurrs when isolated VanX is expressed in Escherichia coli at temperatures lower than 30°C. No cell lysis is observed when VanX is expressed, even in large quantities, in the cell inclusion bodies at 37°C, suggesting that a natively folded VanX is required for lysis. In addition, VanX mutants with suppressed dipeptidase activity do not lyse Escherichia coli cells, confirming that bacteriolysis originates from the dipeptidase activity of VanX. There are also shape changes in Escherichia coli cells undergoing VanX-mediated lysis, these changes may be classified into three classes: bursting, deformation, and leaking fluid | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
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