| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50051503 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_158375 (CHEMBL769576) |
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| IC50 | 58±n/a nM |
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| Citation |  Portevin, B; Benoist, A; Rémond, G; Hervé, Y; Vincent, M; Lepagnol, J; De Nanteuil, G New prolyl endopeptidase inhibitors: in vitro and in vivo activities of azabicyclo[2.2.2]octane, azabicyclo[2.2.1]heptane, and perhydroindole derivatives. J Med Chem39:2379-91 (1996) [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: | PE | PEP | POP | PPCE_HUMAN | PREP | Post-proline cleaving enzyme | Prolyl oligopeptidase |
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| Type: | Enzyme |
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| Mol. Mass.: | 80688.50 |
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| Organism: | Homo sapiens (Human) |
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| Description: | P48147 |
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| Residue: | 710 |
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| Sequence: | MLSLQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR
GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILS
DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTH
DGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAEL
SDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRQSPNYRVINIDFRDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNI
LQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPR
VFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI
TPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE
GYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV
GRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP
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| BDBM50051503 |
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| n/a |
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| Name | BDBM50051503 |
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| Synonyms: | 4,4-Dicyclopropyl-1-[(2S,3aS,7aS)-2-(pyrrolidine-1-carbonyl)-octahydro-indol-1-yl]-butan-1-one | CHEMBL76680 |
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| Type | Small organic molecule |
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| Emp. Form. | C23H36N2O2 |
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| Mol. Mass. | 372.5441 |
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| SMILES | O=C(CCC(C1CC1)C1CC1)N1[C@H]2CCCC[C@H]2C[C@H]1C(=O)N1CCCC1 |
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| Structure | 
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