| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50508977 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_1836618 (CHEMBL4336751) |
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| Ki | 4.0±n/a nM |
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| Citation |  Plescia, J; De Cesco, S; Patrascu, MB; Kurian, J; Di Trani, J; Dufresne, C; Wahba, AS; Janmamode, N; Mittermaier, AK; Moitessier, N Integrated Synthetic, Biophysical, and Computational Investigations of Covalent Inhibitors of Prolyl Oligopeptidase and Fibroblast Activation Protein ?. J Med Chem62:7874-7884 (2019) [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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| BDBM50508977 |
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| n/a |
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| Name | BDBM50508977 |
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| Synonyms: | CHEMBL4451993 |
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| Type | Small organic molecule |
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| Emp. Form. | C21H20N2O3 |
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| Mol. Mass. | 348.3951 |
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| SMILES | O=C[C@@H]1CCCN1C(=O)c1cccc2CN(Cc3ccccc3)C(=O)c12 |r| |
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| Structure | 
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