Reaction Details |
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Target | Prolyl endopeptidase FAP |
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Ligand | BDBM50171650 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_321506 (CHEMBL880566) |
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IC50 | 290±n/a nM |
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Citation | Hu, Y; Ma, L; Wu, M; Wong, MS; Li, B; Corral, S; Yu, Z; Nomanbhoy, T; Alemayehu, S; Fuller, SR; Rosenblum, JS; Rozenkrants, N; Minimo, LC; Ripka, WC; Szardenings, AK; Kozarich, JW; Shreder, KR Synthesis and structure-activity relationship of N-alkyl Gly-boro-Pro inhibitors of DPP4, FAP, and DPP7. Bioorg Med Chem Lett15:4239-42 (2005) [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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BDBM50171650 |
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n/a |
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Name | BDBM50171650 |
Synonyms: | 2-Cyclooctonylamino-1-pyrrolidin-1-yl--2-borandihydroxy-ethanone | CHEMBL382974 |
Type | Small organic molecule |
Emp. Form. | C14H27BN2O3 |
Mol. Mass. | 282.187 |
SMILES | OB(O)[C@@H]1CCCN1C(=O)CNC1CCCCCCC1 |
Structure |
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