| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50135634 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_157490 (CHEMBL765807) |
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| Ki | 0.450000±n/a nM |
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| Citation |  Bal, G; Van der Veken, P; Antonov, D; Lambeir, AM; Grellier, P; Croft, SL; Augustyns, K; Haemers, A Prolylisoxazoles: potent inhibitors of prolyloligopeptidase with antitrypanosomal activity. Bioorg Med Chem Lett13:2875-8 (2003) [PubMed] |
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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 |
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| Synonyms: | PE | PEP | POP | PPCE_HUMAN | PREP | Post-proline cleaving enzyme | Prolyl oligopeptidase |
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| Type: | Enzyme |
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| Mol. Mass.: | 80688.50 |
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| Organism: | Homo sapiens (Human) |
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| Description: | P48147 |
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| Residue: | 710 |
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| Sequence: | MLSLQYPDVYRDETAVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIR
GLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILS
DDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTH
DGKGMFYNSYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAEL
SDDGRYVLLSIREGCDPVNRLWYCDLQQESSGIAGILKWVKLIDNFEGEYDYVTNEGTVF
TFKTNRQSPNYRVINIDFRDPEESKWKVLVPEHEKDVLEWIACVRSNFLVLCYLHDVKNI
LQLHDLTTGALLKTFPLDVGSIVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPR
VFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISI
TPNYSVSRLIFVRHMGGILAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKE
GYTSPKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYG
CSDSKQHFEWLVKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIV
GRSRKQSNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNVDWIP
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| BDBM50135634 |
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| n/a |
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| Name | BDBM50135634 |
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| Synonyms: | (S)-2-[(S)-2-(5-Trimethylsilanyl-isoxazole-3-carbonyl)-pyrrolidine-1-carbonyl]-pyrrolidine-1-carboxylic acid benzyl ester | CHEMBL99305 |
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| Type | Small organic molecule |
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| Emp. Form. | C24H31N3O5Si |
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| Mol. Mass. | 469.6055 |
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| SMILES | C[Si](C)(C)c1cc(no1)C(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)OCc1ccccc1 |
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| Structure | 
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