| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50374386 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_469247 (CHEMBL948947) |
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| IC50 | 5.6±n/a nM |
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| Citation |  Maryanoff, BE; Costanzo, MJ Inhibitors of proteases and amide hydrolases that employ an alpha-ketoheterocycle as a key enabling functionality. Bioorg Med Chem16:1562-95 (2008) [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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| BDBM50374386 |
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| n/a |
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| Name | BDBM50374386 |
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| Synonyms: | CHEMBL269970 |
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| Type | Small organic molecule |
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| Emp. Form. | C26H29N3O3 |
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| Mol. Mass. | 431.5268 |
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| SMILES | O=C([C@@H]1CCCN1CCCc1ccccc1)N1CCC[C@H]1C(=O)c1nc2ccccc2o1 |
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| Structure | 
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