| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50284126 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_632261 (CHEMBL1110123) |
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| IC50 | 8.7±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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| BDBM50284126 |
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| n/a |
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| Name | BDBM50284126 |
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| Synonyms: | (S)-1-((S)-1-(4-phenylbutanoyl)pyrrolidine-2-carbonyl)pyrrolidine-2-carbaldehyde | (S)-1-[(S)-1-(4-Phenyl-butyryl)-pyrrolidine-2-carbonyl]-pyrrolidine-2-carbaldehyde | CHEMBL169572 |
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| Type | Small organic molecule |
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| Emp. Form. | C20H26N2O3 |
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| Mol. Mass. | 342.432 |
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| SMILES | O=C[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CCCc1ccccc1 |
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| Structure | 
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