Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Phospholipids | stimulate | Escherichia coli | |
Triton X-100 | stimulates activity with pro-OmpA-nuclease A or a peptide substrate | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.032 | - |
pro-OmpA-nuclease A | - |
Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | the catalytic domain extends into the periplasmic space and is anchored to the membrane by two transmembrane segments located at the N-terminal end of the protein | Escherichia coli | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
soluble form of the leader peptidase DELTA2-75 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Hybrid protein pro-OmpA-nuclease A + H2O | - |
Escherichia coli | ? | - |
? | |
pro-OmpA-nuclease A + H2O | - |
Escherichia coli | OmpA-nuclease A + ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3 | - |
pro-OmpA-nuclease A | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
5.6 | Escherichia coli |