| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50316822 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_632259 (CHEMBL1110121) |
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| IC50 | 1.05±n/a nM |
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| Citation |  Lawandi, J; Gerber-Lemaire, S; Juillerat-Jeanneret, L; Moitessier, N Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors. J Med Chem53:3423-38 (2010) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Prolyl endopeptidase |
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| Name: | Prolyl endopeptidase |
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| Synonyms: | 3.4.21.26 | PE | PPCE_PIG | PREP | Post-proline cleaving enzyme |
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| Type: | n/a |
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| Mol. Mass.: | 80758.04 |
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| Organism: | Sus scrofa |
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| Description: | n/a |
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| Residue: | 710 |
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| Sequence: | MLSFQYPDVYRDETAIQDYHGHKVCDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR
GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILS
DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTH
DGKGMFYNAYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAEL
SDDGRYVLLSIREGCDPVNRLWYCDLQQESNGITGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRHSPNYRLINIDFTDPEESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLHDVKNT
LQLHDLATGALLKIFPLEVGSVVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPR
VFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI
TPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE
GYTSPKRLTINGGSNGGLLVATCANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLIKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV
GRSRKQNNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNIDWIP
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| BDBM50316822 |
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| n/a |
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| Name | BDBM50316822 |
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| Synonyms: | 3-cyclohexyl-N-((S)-1-oxo-3-phenyl-1-((S)-2-(piperidine-1-carbonyl)pyrrolidin-1-yl)propan-2-yl)propanamide | CHEMBL1087096 |
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| Type | Small organic molecule |
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| Emp. Form. | C28H41N3O3 |
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| Mol. Mass. | 467.6434 |
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| SMILES | O=C(CCC1CCCCC1)N[C@@H](Cc1ccccc1)C(=O)N1CCC[C@H]1C(=O)N1CCCCC1 |r| |
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| Structure | 
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