| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50155838 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_302659 (CHEMBL839948) |
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| Ki | 0.02±n/a nM |
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| Citation |  Jarho, EM; Venäläinen, JI; Huuskonen, J; Christiaans, JA; Garcia-Horsman, JA; Forsberg, MM; Järvinen, T; Gynther, J; Männistö, PT; Wallén, EA A cyclopent-2-enecarbonyl group mimics proline at the P2 position of prolyl oligopeptidase inhibitors. J Med Chem47:5605-7 (2004) [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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| BDBM50155838 |
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| n/a |
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| Name | BDBM50155838 |
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| Synonyms: | (S)-1-((S)-1-(4-phenylbutanoyl)pyrrolidine-2-carbonyl)pyrrolidine-2-carbonitrile | (S)-1-[(S)-1-(4-Phenyl-butyryl)-pyrrolidine-2-carbonyl]-pyrrolidine-2-carbonitrile | CHEMBL189620 |
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| Type | Small organic molecule |
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| Emp. Form. | C20H25N3O2 |
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| Mol. Mass. | 339.4314 |
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| SMILES | O=C(CCCc1ccccc1)N1CCC[C@H]1C(=O)N1CCC[C@H]1C#N |
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| Structure | 
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