| Reaction Details |
|---|
 | Report a problem with these data |
| Target | Acetylcholinesterase |
|---|
| Ligand | BDBM50171928 |
|---|
| Substrate/Competitor | n/a |
|---|
| Meas. Tech. | ChEMBL_303485 (CHEMBL838859) |
|---|
| Ki | >100000±n/a nM |
|---|
| Citation |  Hyatt, JL; Stacy, V; Wadkins, RM; Yoon, KJ; Wierdl, M; Edwards, CC; Zeller, M; Hunter, AD; Danks, MK; Crundwell, G; Potter, PM Inhibition of carboxylesterases by benzil (diphenylethane-1,2-dione) and heterocyclic analogues is dependent upon the aromaticity of the ring and the flexibility of the dione moiety. J Med Chem48:5543-50 (2005) [PubMed] Article |
|---|
| More Info.: | Get all data from this article, Assay Method |
|---|
| |
| Acetylcholinesterase |
|---|
| Name: | Acetylcholinesterase |
|---|
| Synonyms: | ACES_HUMAN | ACHE | Acetylcholinesterase (AChE) | Acetylcholinesterase (human AChE) |
|---|
| Type: | Enzyme |
|---|
| Mol. Mass.: | 67792.70 |
|---|
| Organism: | Homo sapiens (Human) |
|---|
| Description: | P22303 |
|---|
| Residue: | 614 |
|---|
| Sequence: | MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV
SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM
NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV
GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG
VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE
DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY
EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ
YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL
|
|
|
|---|
| BDBM50171928 |
|---|
| n/a |
|---|
| Name | BDBM50171928 |
|---|
| Synonyms: | 1,2-Bis-(5-bromo-thiophen-2-yl)-ethane-1,2-dione | 1,2-bis(5-bromothiophen-2-yl)ethane-1,2-dione | CHEMBL192592 |
|---|
| Type | Small organic molecule |
|---|
| Emp. Form. | C10H4Br2O2S2 |
|---|
| Mol. Mass. | 380.076 |
|---|
| SMILES | Brc1ccc(s1)C(=O)C(=O)c1ccc(Br)s1 |
|---|
| Structure | 
|
|---|
Search and Browse
