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Literature summary extracted from

  • Isaya, G.; Kalousek, F.; Rosenberg, L.E.
    Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase (1992), J. Biol. Chem., 267, 7904-7910.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.59 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
3.4.24.59 Synthetic peptides corresponding to the intermediate octapeptides of human ornithine transcarbamoylase and of Neurospora cytochrome c reductase Fe/S subunit Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.59 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.59 liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.24.59 additional information
-
-
 Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.59 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.59 27
-
 assay at Rattus norvegicus