Reaction Details |
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Target | Prolyl endopeptidase |
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Ligand | BDBM50302967 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_596527 (CHEMBL1039015) |
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IC50 | >100000±n/a nM |
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Citation | Nordhoff, S; Bulat, S; Cerezo-Gálvez, S; Hill, O; Hoffmann-Enger, B; López-Canet, M; Rosenbaum, C; Rummey, C; Thiemann, M; Matassa, VG; Edwards, PJ; Feurer, A The design of potent and selective inhibitors of DPP-4: optimization of ADME properties by amide replacements. Bioorg Med Chem Lett19:6340-5 (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: | 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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BDBM50302967 |
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n/a |
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Name | BDBM50302967 |
Synonyms: | (R)-3-amino-1-((S)-2-(5-cyclopropyl-1,2,4-oxadiazol-3-yl)pyrrolidin-1-yl)-4-(2,4,5-trifluorophenyl)butan-1-one | CHEMBL566419 |
Type | Small organic molecule |
Emp. Form. | C19H21F3N4O2 |
Mol. Mass. | 394.3908 |
SMILES | N[C@@H](CC(=O)N1CCC[C@H]1c1noc(n1)C1CC1)Cc1cc(F)c(F)cc1F |r| |
Structure |
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