Reaction Details |
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Target | Acetylcholinesterase |
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Ligand | BDBM50199541 |
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Substrate/Competitor | n/a |
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Meas. Tech. | ChEMBL_441060 (CHEMBL890218) |
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pH | 5±n/a |
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IC50 | 1002±n/a nM |
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Comments | extracted |
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Citation | He, XC; Feng, S; Wang, ZF; Shi, Y; Zheng, S; Xia, Y; Jiang, H; Tang, XC; Bai, D Study on dual-site inhibitors of acetylcholinesterase: Highly potent derivatives of bis- and bifunctional huperzine B. Bioorg Med Chem15:1394-408 (2007) [PubMed] Article |
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More Info.: | Get all data from this article, Assay Method |
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Acetylcholinesterase |
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Name: | Acetylcholinesterase |
Synonyms: | ACES_RAT | Acetylcholinesterase (AChE) | Acetylcholinesterase and butyrylcholinesterase (AChE and BChE) | Acetylcholinesterase precursor | Acetylcholinesterase, AChE | Ache |
Type: | Enzyme |
Mol. Mass.: | 68193.62 |
Organism: | Rattus norvegicus (rat) |
Description: | P37136 |
Residue: | 614 |
Sequence: | MRPPWYPLHTPSLASPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPV
SAFLGIPFAEPPVGSRRFMPPEPKRPWSGILDATTFQNVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPTSPTPVLIWIYGGGFYSGASSLDVYDGRFLAQVEGTVLVSM
NYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASV
GMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTEL
ISCLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPDALINTGDFQDLQVLVG
VVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPE
DPAHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGY
EIEFIFGLPLDPSLNYTVEERIFAQRLMQYWTNFARTGDPNDPRDSKSPRWPPYTTAAQQ
YVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQERCSDL
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BDBM50199541 |
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n/a |
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Name | BDBM50199541 |
Synonyms: | CHEMBL397501 | N,N-bis(1-oxo-8,15-didehydrolycodinocarbonylmethyl)-cyclopropylamine |
Type | Small organic molecule |
Emp. Form. | C39H47N5O4 |
Mol. Mass. | 649.8216 |
SMILES | CC1=C[C@H]2Cc3[nH]c(=O)ccc3[C@@]3(C1)[C@@H]2CCCN3C(=O)CN(CC(=O)N1CCC[C@@H]2[C@@H]3Cc4[nH]c(=O)ccc4[C@]12CC(C)=C3)C1CC1 |c:50,t:1,TLB:10:11:14:13.2.1,6:5:14:13.2.1,THB:43:42:30:32.33.39| |
Structure |
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