A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion
| Autor: | Paul Cohen, Anne-Marie Leseney, Krishnamurti de Morais Carvalho, Hamadi Boussetta, Carine Joudiou |
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| Rok vydání: | 1992 |
| Předmět: |
Molecular Sequence Data
Substrate Specificity chemistry.chemical_compound Xenopus laevis Endopeptidase activity Animals Protease Inhibitors Amino Acid Sequence Neprilysin Peptide sequence Skin Multidisciplinary Chymotrypsin biology Phosphoramidon Metalloendopeptidases Hydrogen-Ion Concentration Angiotensin II Carboxypeptidase Molecular biology Endopeptidase Hormones body regions chemistry Biochemistry biology.protein Peptides Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 89(1) |
| ISSN: | 0027-8424 |
| Popis: | An endopeptidase was isolated from Xenopus laevis skin secretions. This enzyme, which has an apparent molecular mass of 100 kDa, performs a selective cleavage at the Xaa-Phe, Xaa-Leu, or Xaa-Ile bond (Xaa = Ser, Phe, Tyr, His, or Gly) of a number of peptide hormones, including atrial natriuretic factor, substance P, angiotensin II, bradykinin, somatostatin, neuromedins B and C, and litorin. The peptidase exhibited optimal activity at pH 7.5 and a Km in the micromolar range. No cleavage was produced in vasopressin, ocytocin, minigastrin I, and [Leu5]enkephalin, which include in their sequence an Xaa-Phe, Xaa-Leu, or Xaa-Ile motif. The endopeptidase activity was inhibited by divalent cation chelators and by phosphoramidon only at high concentrations (IC50 = 50 microM), whereas it was insensitive to classical inhibitors of chymotrypsin, angiotensin convertase, and serine and cysteine peptidases, as well as carboxypeptidases. It is hypothesized that this enzyme, which is distinct from neutral endopeptidase (EC 3.4.24.11), constitutes the prototype of a family of related metalloendopeptidases that inactivate peptide substrates by cleavage at the Xaa-Phe, Xaa-Leu, or Xaa-Ile bond. |
| Databáze: | OpenAIRE |
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