Reaction Details |
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Target | Prolyl endopeptidase |
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Ligand | BDBM50155836 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_302659 (CHEMBL839948) |
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Ki | 0.15±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 |
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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BDBM50155836 |
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n/a |
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Name | BDBM50155836 |
Synonyms: | (R)-5-[(S)-2-(2-Hydroxy-acetyl)-pyrrolidine-1-carbonyl]-cyclopent-1-enecarboxylic acid benzylamide | CHEMBL365843 |
Type | Small organic molecule |
Emp. Form. | C20H24N2O4 |
Mol. Mass. | 356.4156 |
SMILES | OCC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCC=C1C(=O)NCc1ccccc1 |c:15| |
Structure |
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