Ecadotril
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").
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| IUPAC name
Benzyl N-[(2S)-3-(acetylsulfanyl)-2-benzylpropanoyl]glycinate | |
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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). | |
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See also
References
- 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.
- 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.
- 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.
- 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.
- 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.