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_495212 (CHEMBL998642) |
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IC50 | 30±n/a nM |
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Citation | Kánai, K; Arányi, P; Böcskei, Z; Ferenczy, G; Harmat, V; Simon, K; Bátori, S; Náray-Szabo, G; Hermecz, I Prolyl oligopeptidase inhibition by N-acyl-pro-pyrrolidine-type molecules. J Med Chem51:7514-22 (2009) [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: | PPCE_RAT | Prep |
Type: | PROTEIN |
Mol. Mass.: | 80731.99 |
Organism: | Rattus norvegicus |
Description: | ChEMBL_1336163 |
Residue: | 710 |
Sequence: | MLSFQYPDVYRDETSVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR
GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLS
DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTH
DGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDVLCAEFPDEPKWMGGAEL
SDDGRYVLLSIWEGCDPVNRLWYCDLQQGSNGINGILKWVKLIDNFEGEYDYITNEGTVF
TFKTNRNSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLRNVKNI
LQLHDLTTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTREELEPR
VFREVTVKGIDASDYQTIQVFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI
TPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE
GYTTSKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKFTIGHAWTTDYG
CSDSKQHFEWLLKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV
GRSRKQSNPLLIHVDTKAGHGPGKPTAKVIEEVSDMFAFIARCLNIEWIQ
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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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