EC Number   |
Natural Substrates |
|---|
   3.4.17.12 | Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O |
bradykinin |
| 3.4.17.12 | EGF + H2O |
EGF, epidermal growth factor |
| 3.4.17.12 | epidermal growth factor + H2O |
- |
| 3.4.17.12 | more |
the enzyme could inactivate or modulate the activity of peptide hormones either before or after their interaction with plasma membrane receptors |
| 3.4.17.12 | more |
the enzyme controls the activity of kinins in the kidney, is involved in inflammation, and participates in the metabolism of growth factors that contain C-terminal Arg or Lys residues, e.g. the epidermal growth factor, the nerve growth factor, the hypatocyte growth factor, the macrophage-stimulating protein, or erythropoietin |
| 3.4.17.12 | more |
the enzyme may be responsible for control of kinins and epidermal growth factor as well as of EGF-like peptides |
| 3.4.17.12 | more |
the enzyme might be involved in regulating the biological effects of complement anaphylatoxins at sites of tissue injury |
| 3.4.17.12 | more |
the enzyme regulates peptide hormones and growth factors at the cell surface, and is active in the degradation of extracellular proteins in the membrane |
| 3.4.17.12 | more |
using small substrates of the form benzoyl-Xaa-Arg CPM has the highest catalytic efficiency for substrates with the nonpolar aliphatic residues Ala and Met and aromatic amino acids (Phe, Tyr, Trp) in the penultimate place and the lowest with branched side chains (Ile) |
