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Literature summary for 3.4.11.5 extracted from
- Hydrolases from Neisseria gonorrhoeae. The study of gonocosin, an aminopeptidase-P, a proline iminopeptidase, and an asparaginase (1980), J. Biol. Chem., 255, 1704-1710.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| dithiothreitol | activity enhancement | Neisseria gonorrhoeae |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cd2+ | - |
Neisseria gonorrhoeae | |
| Hg2+ | - |
Neisseria gonorrhoeae | |
| N-ethylmaleimide | - |
Neisseria gonorrhoeae | |
| p-chloromercuribenzoate | - |
Neisseria gonorrhoeae | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Neisseria gonorrhoeae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-prolyl-peptide + H2O | hydrolytic activity decreases with increasing chain length | Neisseria gonorrhoeae | L-proline + peptide | - |
? | |
| L-prolyl-peptide + H2O | influence of amino acid adjacent to N-terminal L-Pro on rate of hydrolysis | Neisseria gonorrhoeae | L-proline + peptide | - |
? | |
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