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. | ChEMBL_876941 (CHEMBL2185389) |
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IC50 | 130±n/a nM |
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Citation | Van der Veken, P; Fülöp, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K P2-substituted N-acylprolylpyrrolidine inhibitors of prolyl oligopeptidase: biochemical evaluation, binding mode determination, and assessment in a cellular model of synucleinopathy. J Med Chem55:9856-67 (2012) [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: | 3.4.21.26 | PE | PPCE_PIG | PREP | Post-proline cleaving enzyme |
Type: | n/a |
Mol. Mass.: | 80758.04 |
Organism: | Sus scrofa |
Description: | n/a |
Residue: | 710 |
Sequence: | MLSFQYPDVYRDETAIQDYHGHKVCDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR
GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILS
DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTH
DGKGMFYNAYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAEL
SDDGRYVLLSIREGCDPVNRLWYCDLQQESNGITGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRHSPNYRLINIDFTDPEESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLHDVKNT
LQLHDLATGALLKIFPLEVGSVVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPR
VFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI
TPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE
GYTSPKRLTINGGSNGGLLVATCANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLIKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV
GRSRKQNNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNIDWIP
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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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