Ecadotril Explained

Ecadotril is a neutral endopeptidase inhibitor ((NEP^[1]) EC 3.4.24.11^[2]) and determined by the presence of peptidase family M13 as a neutral endopeptidase inhibited by phosphoramidon. Ecadotril is the (S)-enantiomer of racecadotril. NEP-like enzymes include the endothelin-converting enzymes.^[3] The peptidase M13 family believed to activate or inactivate oligopeptide (pro)-hormones such as opioid peptides,^[3] neprilysin^[3] is another member of this group, in the case of the metallopeptidases and aspartic, the nucleophiles clan or family for example MA, is an activated water molecule.^[1] The peptidase domain for members of this family also contains a bacterial member and resembles that of thermolysin the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH.^[4] Thermolysin complexed with the inhibitor (S)-thiorphan are isomeric thiol-containing inhibitors of endopeptidase EC 24-11^[5] (also called "enkephalinase").

See also

• RB-101
• Candoxatril

Notes and References

1. Le Moual H, Roques BP, Crine P, Boileau G . Substitution of potential metal-coordinating amino acid residues in the zinc-binding site of endopeptidase-24.11. . FEBS Lett. . 324 . 2 . 196–200 . June 1993 . 8099556 . 10.1016/0014-5793(93)81392-D . free .
2. Malfroy B, Schofield PR, Kuang WJ, Seeburg PH, Mason AJ, Henzel WJ . Molecular cloning and amino acid sequence of rat enkephalinase . Biochemical and Biophysical Research Communications . 144 . 1 . 59–66 . April 1987 . 3555489 . 10.1016/S0006-291X(87)80475-8 .
3. Turner AJ, Isaac RE, Coates D . The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function. . BioEssays . 23 . 3 . 261–9 . March 2001 . 11223883 . 10.1002/1521-1878(200103)23:3<261::AID-BIES1036>3.0.CO;2-K .
4. Rudner DZ, Fawcett P, Losick R . A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors. . Proc Natl Acad Sci USA . 96 . 26 . 14765–14770 . December 1999 . 10611287 . 10.1073/pnas.96.26.14765 . 24722. free .
5. S. L. Roderick . M. C. Fournie-Zaluski . B. P. Roques . B. W. Matthews . Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin . Biochemistry . 28 . 4 . 1493–7 . February 1989 . 2719912 . 10.1021/bi00430a011 .