| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50431242 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_1335497 (CHEMBL3239282) |
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| IC50 | 990±n/a nM |
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| Citation |  Jansen, K; Heirbaut, L; Verkerk, R; Cheng, JD; Joossens, J; Cos, P; Maes, L; Lambeir, AM; De Meester, I; Augustyns, K; Van der Veken, P Extended structure-activity relationship and pharmacokinetic investigation of (4-quinolinoyl)glycyl-2-cyanopyrrolidine inhibitors of fibroblast activation protein (FAP). J Med Chem57:3053-74 (2014) [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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| BDBM50431242 |
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| n/a |
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| Name | BDBM50431242 |
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| Synonyms: | CHEMBL2333026 |
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| Type | Small organic molecule |
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| Emp. Form. | C13H18BN3O4 |
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| Mol. Mass. | 291.111 |
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| SMILES | C[C@@H](NC(=O)c1ccncc1)C(=O)N1CCC[C@H]1B(O)O |r| |
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| Structure | 
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