| Reaction Details |
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 | Report a problem with these data |
| Target | Prolyl endopeptidase |
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| Ligand | BDBM50251786 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_488667 (CHEMBL988357) |
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| IC50 | >10000±n/a nM |
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| Citation |  Sattigeri, JA; Andappan, MM; Kishore, K; Thangathirupathy, S; Sundaram, S; Singh, S; Sharma, S; Davis, JA; Chugh, A; Bansal, VS Discovery of conformationally rigid 3-azabicyclo[3.1.0]hexane-derived dipeptidyl peptidase-IV inhibitors. Bioorg Med Chem Lett18:4087-91 (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 |
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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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| BDBM50251786 |
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| n/a |
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| Name | BDBM50251786 |
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| Synonyms: | (2S,4S)-1-(2-((1S,5R,6s)-3-(2-cyano-3-(trifluoromethyl)phenyl)-3-aza-bicyclo[3.1.0]hexan-6-ylamino)acetyl)-4-fluoropyrrolidine-2-carbonitrile | CHEMBL520266 |
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| Type | Small organic molecule |
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| Emp. Form. | C20H19F4N5O |
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| Mol. Mass. | 421.3914 |
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| SMILES | F[C@H]1C[C@@H](C#N)N(C1)C(=O)CN[C@@H]1[C@H]2CN(C[C@@H]12)c1cccc(c1C#N)C(F)(F)F |r| |
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| Structure | 
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