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Literature summary for 3.4.21.89 extracted from
- Synthesis of precursor maltose-binding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo (1992), J. Biol. Chem., 267, 1231-1238.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | - |
Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | although the enzyme is unable to cleave an X-Pro bond, a proline at-1 does not prevent the enzyme from recognizing the normal processing site | Escherichia coli | ? | - |
? |  |
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