IUPAC name
Benzyl N-[(2S)-3-(acetylsulfanyl)-2-benzylpropanoyl]glycinate
3D model (JSmol)
Molar mass 385.48 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references

Ecadotril is a neutral endopeptidase inhibitor ((NEP[1]) EC[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


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