Reaction Details |
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Target | Prolyl endopeptidase FAP |
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Ligand | BDBM50316820 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_876940 (CHEMBL2185388) |
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IC50 | >100000±n/a nM |
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Citation | Van der Veken, P; Fülöp, V; Rea, D; Gerard, M; Van Elzen, R; Joossens, J; Cheng, JD; Baekelandt, V; De Meester, I; Lambeir, AM; Augustyns, K P2-substituted N-acylprolylpyrrolidine inhibitors of prolyl oligopeptidase: biochemical evaluation, binding mode determination, and assessment in a cellular model of synucleinopathy. J Med Chem55:9856-67 (2012) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Prolyl endopeptidase FAP |
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Name: | Prolyl endopeptidase FAP |
Synonyms: | Fap | Fibroblast activation protein (FAP) | SEPR_MOUSE | Seprase |
Type: | Enzyme |
Mol. Mass.: | 87949.14 |
Organism: | Mus musculus (Mouse) |
Description: | P97321 |
Residue: | 761 |
Sequence: | MKTWLKTVFGVTTLAALALVVICIVLRPSRVYKPEGNTKRALTLKDILNGTFSYKTYFPN
WISEQEYLHQSEDDNIVFYNIETRESYIILSNSTMKSVNATDYGLSPDRQFVYLESDYSK
LWRYSYTATYYIYDLQNGEFVRGYELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPP
FQITYTGRENRIFNGIPDWVYEEEMLATKYALWWSPDGKFLAYVEFNDSDIPIIAYSYYG
DGQYPRTINIPYPKAGAKNPVVRVFIVDTTYPHHVGPMEVPVPEMIASSDYYFSWLTWVS
SERVCLQWLKRVQNVSVLSICDFREDWHAWECPKNQEHVEESRTGWAGGFFVSTPAFSQD
ATSYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAIYIFRVTQDSLFYSSNEFEGYPG
RRNIYRISIGNSPPSKKCVTCHLRKERCQYYTASFSYKAKYYALVCYGPGLPISTLHDGR
TDQEIQVLEENKELENSLRNIQLPKVEIKKLKDGGLTFWYKMILPPQFDRSKKYPLLIQV
YGGPCSQSVKSVFAVNWITYLASKEGIVIALVDGRGTAFQGDKFLHAVYRKLGVYEVEDQ
LTAVRKFIEMGFIDEERIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIY
SERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNA
QVDFQAMWYSDQNHGISSGRSQNHLYTHMTHFLKQCFSLSD
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BDBM50316820 |
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n/a |
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Name | BDBM50316820 |
Synonyms: | (S)-benzyl 2-(pyrrolidine-1-carbonyl)pyrrolidine-1-carboxylate | CHEMBL1088406 |
Type | Small organic molecule |
Emp. Form. | C17H22N2O3 |
Mol. Mass. | 302.3682 |
SMILES | O=C(OCc1ccccc1)N1CCC[C@H]1C(=O)N1CCCC1 |r| |
Structure |
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