Ecadotril

Ecadotril
Identifiers
CAS number 112573-73-6
PubChem 60561
ChemSpider 54591
SMILES
InChI
Properties
Molecular formula C21H23NO4S
Molar mass 385.48 g mol−1
Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Infobox references

Ecadotril 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 endothelinconverting 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

References

  1. ^ a b 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”. Biochemistry. 144 (1): 59-66. doi:10.1016/S0006-291X(87)80475-8. PMID 3555489.
  3. ^ a b c 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)23:33.0.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 U S A. 96 (26): 14765-14770. doi:10.1073/pnas.96.26.14765. 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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