The Enterococcus faecalis extracellular metalloendopeptidase (EC 3.4.24.30; coccolysin) inactivates human endothelin at bonds involving hydrophobic amino acid residues.
The extracellular metalloendopeptidase (EC 3.4.24.30; 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.
Mäkinen
P L
PL
Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor 48109.
Mäkinen
K K
KK
D000595:Amino Acid Sequence; D001665:Binding Sites; D016232:Endothelins / Q000037:antagonists & inhibitors* / Q000235:genetics; D013293:Enterococcus faecalis / Q000201:enzymology; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D008666:Metalloendopeptidases / Q000378:metabolism* / Q000494:pharmacology; D008969:Molecular Sequence Data; D013379:Substrate Specificity
D016232:Endothelins; D008666:Metalloendopeptidases; C100310:Streptococcus faecalis metalloproteinase