Ecadotril

Ecadotril

Ecadotril
Identifiers
CAS number
PubChem
ChemSpider
ChEMBL
Jmol-3D images Image 1
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 (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.  
  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.  
  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.  
  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.  
  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.