Share to:

 

Ecadotril

Ecadotril
Names
Preferred IUPAC name
Benzyl [(2S)-3-(acetylsulfanyl)-2-benzylpropanamido]acetate
Identifiers
3D model (JSmol)
ChEMBL
ChemSpider
UNII
  • InChI=1S/C21H23NO4S/c1-16(23)27-15-19(12-17-8-4-2-5-9-17)21(25)22-13-20(24)26-14-18-10-6-3-7-11-18/h2-11,19H,12-15H2,1H3,(H,22,25)/t19-/m1/s1
    Key: ODUOJXZPIYUATO-LJQANCHMSA-N
  • InChI=1/C21H23NO4S/c1-16(23)27-15-19(12-17-8-4-2-5-9-17)21(25)22-13-20(24)26-14-18-10-6-3-7-11-18/h2-11,19H,12-15H2,1H3,(H,22,25)/t19-/m1/s1
    Key: ODUOJXZPIYUATO-LJQANCHMBY
  • O=C(SC[C@H](C(=O)NCC(=O)OCc1ccccc1)Cc2ccccc2)C
Properties
C21H23NO4S
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).

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

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. Bibcode:1993FEBSL.324..196L. 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. ^ 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)23:3<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. Bibcode:1999PNAS...9614765R. 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.
Kembali kehalaman sebelumnya