Reaction Details |
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Target | Prolyl endopeptidase FAP |
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Ligand | BDBM50200729 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_632272 (CHEMBL1110134) |
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Ki | 29±n/a nM |
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Citation | Lawandi, J; Gerber-Lemaire, S; Juillerat-Jeanneret, L; Moitessier, N Inhibitors of prolyl oligopeptidases for the therapy of human diseases: defining diseases and inhibitors. J Med Chem53:3423-38 (2010) [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: | 170 kDa melanoma membrane-bound gelatinase | FAP | Fibroblast Activation Protein (FAP) | Fibroblast activation protein alpha | Integral membrane serine protease | SEPR_HUMAN | Seprase |
Type: | Enzyme |
Mol. Mass.: | 87712.48 |
Organism: | Homo sapiens (Human) |
Description: | Q12884 |
Residue: | 760 |
Sequence: | MKTWVKIVFGVATSAVLALLVMCIVLRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPN
WISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSK
LWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPP
FQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYG
DEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVT
DERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYD
AISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPG
RRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGR
TDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQV
YGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQ
ITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVY
TERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNA
QVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD
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BDBM50200729 |
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n/a |
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Name | BDBM50200729 |
Synonyms: | (R)-1-(2-(2,5-dichlorobenzamido)acetyl)pyrrolidin-2-ylboronic acid | CHEMBL386890 |
Type | Small organic molecule |
Emp. Form. | C13H15BCl2N2O4 |
Mol. Mass. | 344.986 |
SMILES | OB(O)[C@@H]1CCCN1C(=O)CNC(=O)c1cc(Cl)ccc1Cl |
Structure |
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