The Enterococcus faecalis extracellular metalloendopeptidase (EC; coccolysin) inactivates human endothelin at bonds involving hydrophobic amino acid residues

Biochem Biophys Res Commun. 1994 Apr 29;200(2):981-5. doi: 10.1006/bbrc.1994.1546.


The extracellular metalloendopeptidase (EC; coccolysin) from Enterococcus faecalis (Strain OG1-10) inactivates human endothelin-1 by hydrolyzing the peptide primarily at the Ser5-Leu6 and the His16-Leu17 bonds and the human big endothelin at several bonds involving hydrophobic amino acid residues. The big endothelin fragment 22-38 was also hydrolyzed at a high rate. The degradation of endothelin by coccolysin resembles the peptidolytic processing of endothelin by thermolysin. Because E. faecalis is associated with a large number of infectious diseases, it is possible that the manifestation of inflammatory conditions in the presence of this organism is related to the coccolysin-catalyzed inactivation of endothelin.

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Endothelins / antagonists & inhibitors*
  • Endothelins / genetics
  • Enterococcus faecalis / enzymology
  • Humans
  • Hydrolysis
  • In Vitro Techniques
  • Metalloendopeptidases / metabolism*
  • Metalloendopeptidases / pharmacology
  • Molecular Sequence Data
  • Substrate Specificity


  • Endothelins
  • Metalloendopeptidases
  • Streptococcus faecalis metalloproteinase