Reaction Details |
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Target | Prolyl endopeptidase |
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Ligand | BDBM50135633 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_469259 (CHEMBL949941) |
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Ki | 4±n/a nM |
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Citation | Maryanoff, BE; Costanzo, MJ Inhibitors of proteases and amide hydrolases that employ an alpha-ketoheterocycle as a key enabling functionality. Bioorg Med Chem16:1562-95 (2008) [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: | PE | PEP | POP | PPCE_HUMAN | PREP | Post-proline cleaving enzyme | Prolyl oligopeptidase |
Type: | Enzyme |
Mol. Mass.: | 80688.50 |
Organism: | Homo sapiens (Human) |
Description: | P48147 |
Residue: | 710 |
Sequence: | MLSLQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR
GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILS
DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTH
DGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAEL
SDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRQSPNYRVINIDFRDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNI
LQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPR
VFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI
TPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE
GYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV
GRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP
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BDBM50135633 |
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n/a |
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Name | BDBM50135633 |
Synonyms: | (S)-2-[(S)-2-(5-Benzyloxymethyl-isoxazole-3-carbonyl)-pyrrolidine-1-carbonyl]-pyrrolidine-1-carboxylic acid benzyl ester | (S)-benzyl 2-((S)-2-(5-(benzyloxymethyl)isoxazole-3-carbonyl)pyrrolidine-1-carbonyl)pyrrolidine-1-carboxylate | CHEMBL318284 |
Type | Small organic molecule |
Emp. Form. | C29H31N3O6 |
Mol. Mass. | 517.5729 |
SMILES | O=C(OCc1ccccc1)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)c1cc(COCc2ccccc2)on1 |
Structure |
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