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Literature summary for 3.4.21.89 extracted from
- Determination of the kinetic parameters of Escherichia coli leader peptidase activity using a continuous assay: the pH dependence and time-dependent inhibition by beta-lactams are consistent with a novel serine protease mechanism (1994), Biochemistry, 33, 8347-8354.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| beta-lactams | - |
Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| Cleavage of hydrophobic, N-terminal signal or leader sequences | mechanism | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | family of serine proteases that lacks a complete catalytic triad | Escherichia coli | ? | - |
? |  |
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