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Literature summary for 3.4.24.59 extracted from
- Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase (1992), J. Biol. Chem., 267, 7904-7910.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no inhibition by peptides lacking the amino-terminal hydrophobic residue, while substitution of such a residue by a polar amino acid causes a 10fold reduction in the efficiency of MIP inhibition | Rattus norvegicus | |
| Synthetic peptides | corresponding to the intermediate octapeptides of human ornithine transcarbamoylase and of Neurospora cytochrome c reductase Fe/S subunit | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Rattus norvegicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Proteins with the octapeptide Phe-Xaa-Xaa-Ser-Xaa-Xaa-Xaa-Xaa at the amino termini + H2O | amino-terminal octapeptide can be cleaved only within the structural context of twice-cleaved precursors | Rattus norvegicus | Protein + Phe-Xaa-Xaa-Ser-Xaa-Xaa-Xaa-Xaa | - |
? |  |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 27 | - |
assay at | Rattus norvegicus |
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Release 2023.1 (January 2023)
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