Reaction Details |
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Target | Prolyl endopeptidase |
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Ligand | BDBM50170682 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_632259 (CHEMBL1110121) |
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Ki | 0.36±n/a nM |
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Citation | Lawandi, J; Gerber-Lemaire, S; Juillerat-Jeanneret, L; Moitessier, N Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors. J Med Chem53:3423-38 (2010) [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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BDBM50170682 |
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n/a |
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Name | BDBM50170682 |
Synonyms: | (S)-1-((S)-1-(3-((S)-2-(cyclopentanecarbonyl)pyrrolidine-1-carbonyl)benzoyl)pyrrolidine-2-carbonyl)pyrrolidine-2-carbonitrile | (S)-1-{(S)-1-[3-((S)-2-Cyclopentanecarbonyl-pyrrolidine-1-carbonyl)-benzoyl]-pyrrolidine-2-carbonyl}-pyrrolidine-2-carbonitrile | CHEMBL191572 |
Type | Small organic molecule |
Emp. Form. | C28H34N4O4 |
Mol. Mass. | 490.594 |
SMILES | O=C(C1CCCC1)[C@@H]1CCCN1C(=O)c1cccc(c1)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C#N |
Structure |
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