Reaction Details |
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Target | Prolyl endopeptidase |
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Ligand | BDBM50051539 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEBML_157469 |
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IC50 | 15±n/a nM |
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Citation | Vendeville, S; Bourel, L; Davioud-Charvet, E; Grellier, P; Deprez, B; Sergheraert, C Automated parallel synthesis of a tetrahydroisoquinolin-based library: potential prolyl endopeptidase inhibitors. Bioorg Med Chem Lett9:437-42 (1999) [PubMed] |
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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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BDBM50051539 |
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n/a |
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Name | BDBM50051539 |
Synonyms: | (S)-4-phenyl-1-(2-(pyrrolidine-1-carbonyl)pyrrolidin-1-yl)butan-1-one | 4-Phenyl-1-[(S)-2-(pyrrolidine-1-carbonyl)-pyrrolidin-1-yl]-butan-1-one | 4-Phenyl-1-[2-(pyrrolidine-1-carbonyl)-pyrrolidin-1-yl]-butan-1-one | CHEMBL289651 | SUAM-1221 |
Type | Small organic molecule |
Emp. Form. | C19H26N2O2 |
Mol. Mass. | 314.4219 |
SMILES | O=C(CCCc1ccccc1)N1CCC[C@H]1C(=O)N1CCCC1 |r| |
Structure |
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