| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50075125 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEBML_157469 |
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| IC50 | 23±n/a nM |
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| Citation |  Vendeville, S; Bourel, L; Davioud-Charvet, E; Grellier, P; Deprez, B; Sergheraert, C Automated parallel synthesis of a tetrahydroisoquinolin-based library: potential prolyl endopeptidase inhibitors. Bioorg Med Chem Lett9:437-42 (1999) [PubMed] |
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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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| BDBM50075125 |
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| n/a |
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| Name | BDBM50075125 |
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| Synonyms: | ((1S,2S)-2-Phenyl-cyclopropyl)-[(S)-3-(pyrrolidine-1-carbonyl)-3,4-dihydro-1H-isoquinolin-2-yl]-methanone | CHEMBL139696 |
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| Type | Small organic molecule |
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| Emp. Form. | C24H26N2O2 |
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| Mol. Mass. | 374.4754 |
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| SMILES | O=C([C@H]1C[C@@H]1c1ccccc1)N1Cc2ccccc2C[C@H]1C(=O)N1CCCC1 |
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| Structure | 
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