Reaction Details |
| Report a problem with these data |
Target | Prolyl endopeptidase |
---|
Ligand | BDBM50155839 |
---|
Substrate/Competitor | n/a |
---|
Meas. Tech. | ChEMBL_302659 (CHEMBL839948) |
---|
Ki | 0.03±n/a nM |
---|
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 |
---|
More Info.: | Get all data from this article, Assay Method |
---|
|
Prolyl endopeptidase |
---|
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
|
|
|
BDBM50155839 |
---|
n/a |
---|
Name | BDBM50155839 |
Synonyms: | (S)-1-[(R)-2-(4-Phenyl-butyryl)-cyclopent-2-enecarbonyl]-pyrrolidine-2-carbonitrile | CHEMBL185848 |
Type | Small organic molecule |
Emp. Form. | C21H24N2O2 |
Mol. Mass. | 336.4275 |
SMILES | O=C(CCCc1ccccc1)C1=CCC[C@H]1C(=O)N1CCC[C@H]1C#N |t:12| |
Structure |
|