| Reaction Details |
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 | Report a problem with these data |
| Target | Fatty-acid amide hydrolase 1 |
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| Ligand | BDBM50323053 |
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| Substrate/Competitor | n/a |
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| Meas. Tech. | ChEMBL_643589 (CHEMBL1212453) |
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| IC50 | >50000±n/a nM |
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| Citation |  Gattinoni, S; Simone, CD; Dallavalle, S; Fezza, F; Nannei, R; Battista, N; Minetti, P; Quattrociocchi, G; Caprioli, A; Borsini, F; Cabri, W; Penco, S; Merlini, L; Maccarrone, M A new group of oxime carbamates as reversible inhibitors of fatty acid amide hydrolase. Bioorg Med Chem Lett20:4406-11 (2010) [PubMed] Article |
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| More Info.: | Get all data from this article, Assay Method |
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| Fatty-acid amide hydrolase 1 |
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| Name: | Fatty-acid amide hydrolase 1 |
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| Synonyms: | Anandamide amidohydrolase | Anandamide amidohydrolase 1 | FAAH1_MOUSE | Faah | Faah1 | Fatty Acid Amide Hydrolase | Fatty-acid amide hydrolase (FAAH) | Fatty-acid amide hydrolase 1 | Oleamide hydrolase 1 |
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| Type: | Hydrolase; single-pass membrane protein; homodimer |
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| Mol. Mass.: | 63227.28 |
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| Organism: | Mus musculus (mouse) |
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| Description: | Mouse brain membranes were used in the assay. |
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| Residue: | 579 |
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| Sequence: | MVLSEVWTALSGLSGVCLACSLLSAAVVLRWTRSQTARGAVTRARQKQRAGLETMDKAVQ
RFRLQNPDLDSEALLALPLLQLVQKLQSGELSPEAVLFTYLGKAWEVNKGTNCVTSYLTD
CETQLSQAPRQGLLYGVPVSLKECFSYKGHASTLGLSLNEGVTSESDCVVVQVLKLQGAV
PFVHTNVPQSMLSYDCSNPLFGQTMNPWKPSKSPGGSSGGEGALIGSGGSPLGLGTDIGG
SIRFPSAFCGICGLKPTGNRLSKSGLKSCVYGQTAVQLSVGPMARDVDSLALCMKALLCE
DLFRLDSTIPPLPFREEIYRSSRPLRVGYYETDNYTMPTPAMRRAVMETKQSLEAAGHTL
VPFLPNNIPYALEVLSAGGLFSDGGCSFLQNFKGDFVDPCLGDLVLVLKLPRWFKKLLSF
LLKPLFPRLAAFLNSMCPRSAEKLWELQHEIEMYRQSVIAQWKAMNLDVVLTPMLGPALD
LNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMEHYKGYFGDMWDNILKKGMK
KGIGLPVAVQCVALPWQEELCLRFMREVERLMTPEKRPS
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| BDBM50323053 |
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| n/a |
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| Name | BDBM50323053 |
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| Synonyms: | 4-Phenyl-cyclohexanone, O-(phenylaminocarbonyl)oxime | CHEMBL1210039 |
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| Type | Small organic molecule |
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| Emp. Form. | C19H20N2O2 |
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| Mol. Mass. | 308.3743 |
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| SMILES | O=[#6](-[#7]-c1ccccc1)-[#8]\[#7]=[#6]-1\[#6]-[#6]-[#6](-[#6]-[#6]-1)-c1ccccc1 |
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| Structure | 
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