| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50193665 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_632259 (CHEMBL1110121) |
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| IC50 | 1.2±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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| BDBM50193665 |
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| n/a |
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| Name | BDBM50193665 |
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| Synonyms: | 1-((2R,5S)-2-tert-butyl-5-(pyrrolidine-1-carbonyl)pyrrolidin-1-yl)-4-phenylbutan-1-one | CHEMBL375794 |
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| Type | Small organic molecule |
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| Emp. Form. | C23H34N2O2 |
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| Mol. Mass. | 370.5283 |
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| SMILES | CC(C)(C)[C@H]1CC[C@H](N1C(=O)CCCc1ccccc1)C(=O)N1CCCC1 |
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| Structure | 
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