| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50200723 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_422119 (CHEMBL908233) |
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| Ki | 2.8±n/a nM |
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| Citation |  Tran, T; Quan, C; Edosada, CY; Mayeda, M; Wiesmann, C; Sutherlin, D; Wolf, BB Synthesis and structure-activity relationship of N-acyl-Gly-, N-acyl-Sar- and N-blocked-boroPro inhibitors of FAP, DPP4, and POP. Bioorg Med Chem Lett17:1438-42 (2007) [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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| BDBM50200723 |
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| n/a |
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| Name | BDBM50200723 |
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| Synonyms: | (R)-1-(2-(1-oxoisoindolin-2-yl)acetyl)pyrrolidin-2-ylboronic acid | CHEMBL387050 |
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| Type | Small organic molecule |
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| Emp. Form. | C14H17BN2O4 |
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| Mol. Mass. | 288.107 |
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| SMILES | OB(O)[C@@H]1CCCN1C(=O)CN1Cc2ccccc2C1=O |
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| Structure | 
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