Reaction Details |
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Target | Prolyl endopeptidase |
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Ligand | BDBM50155838 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_1336165 (CHEMBL3241125) |
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Ki | 0.023000±n/a nM |
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Citation | Kallinen, A; Todorov, B; Kallionpää, R; Bäck, S; Sarparanta, M; Raki, M; García-Horsman, JA; Bergström, KA; Wallén, EA; Männistö, PT; Airaksinen, AJ Synthesis and biological evaluation of novel (123)I-labeled 4-(4-iodophenyl)butanoyl-L-prolyl-(2S)-pyrrolidines for imaging prolyl oligopeptidase in vivo. Eur J Med Chem79:436-45 (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 |
Synonyms: | PE | PEP | POP | PPCE_HUMAN | PREP | Post-proline cleaving enzyme | Prolyl oligopeptidase |
Type: | Enzyme |
Mol. Mass.: | 80688.50 |
Organism: | Homo sapiens (Human) |
Description: | P48147 |
Residue: | 710 |
Sequence: | MLSLQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR
GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILS
DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTH
DGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAEL
SDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRQSPNYRVINIDFRDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNI
LQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPR
VFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI
TPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE
GYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV
GRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP
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BDBM50155838 |
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n/a |
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Name | BDBM50155838 |
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 |
Type | Small organic molecule |
Emp. Form. | C20H25N3O2 |
Mol. Mass. | 339.4314 |
SMILES | O=C(CCCc1ccccc1)N1CCC[C@H]1C(=O)N1CCC[C@H]1C#N |
Structure |
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