Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-24110
Proc Natl Acad Sci U S A 1992 Jan 01;891:84-8.
Show Gene links Show Anatomy links

A peptide-hormone-inactivating endopeptidase in Xenopus laevis skin secretion.

Carvalho KM , Joudiou C , Boussetta H , Leseney AM , Cohen P .


???displayArticle.abstract???
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.

???displayArticle.pubmedLink??? 1729723
???displayArticle.pmcLink??? PMC48180
???displayArticle.link??? Proc Natl Acad Sci U S A


Species referenced: Xenopus laevis
Genes referenced: avp bdkrb2 sst.1 tac1

References [+] :
Almenoff, Biochemical and immunological properties of a membrane-bound brain metalloendopeptidase: comparison with thermolysin-like kidney neutral metalloendopeptidase. 1984, Pubmed