Reaction Details |
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Target | Prolyl endopeptidase |
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Ligand | BDBM50003020 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_1335101 (CHEMBL3239608) |
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IC50 | >67000±n/a nM |
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Citation | Biftu, T; Sinha-Roy, R; Chen, P; Qian, X; Feng, D; Kuethe, JT; Scapin, G; Gao, YD; Yan, Y; Krueger, D; Bak, A; Eiermann, G; He, J; Cox, J; Hicks, J; Lyons, K; He, H; Salituro, G; Tong, S; Patel, S; Doss, G; Petrov, A; Wu, J; Xu, SS; Sewall, C; Zhang, X; Zhang, B; Thornberry, NA; Weber, AE Omarigliptin (MK-3102): a novel long-acting DPP-4 inhibitor for once-weekly treatment of type 2 diabetes. J Med Chem57:3205-12 (2014) [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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BDBM50003020 |
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n/a |
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Name | BDBM50003020 |
Synonyms: | MK-3102 | OMARIGLIPTIN | US10155775, Omarigliptin | US10479798, Compound MK3102 | US10822319, Compound Omarigliptin |
Type | Small organic molecule |
Emp. Form. | C17H20F2N4O3S |
Mol. Mass. | 398.428 |
SMILES | CS(=O)(=O)n1cc2CN(Cc2n1)[C@H]1CO[C@@H]([C@@H](N)C1)c1cc(F)ccc1F |r| |
Structure |
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