Article
Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates.
Biochemistry - 20 Aug 1996
Hosea N A, Radić Z, Tsigelny I, Berman H A, Quinn D M, Taylor P
Abstract excerpt
Through site-specific mutagenesis, we examined the determinants on acetylcholinesterase which govern the specificity and reactivity of three classes of substrates: enantiomeric alkyl phosphonates, trifluoromethyl acetophenones, and carboxyl esters. By employing cationic and uncharged pairs of enantiomeric alkyl methylphosphonyl thioates of known absolute stereochemistry, we find that an aspartate residue near the...
Topics
- Acetylcholinesterase
- Animals
- Aspartic Acid
- Cations
- Cell Line
- Cholinesterase Inhibitors
- Diffusion
- Electrochemistry
- Humans
- Mutation
- Organophosphorus Compounds
- Stereoisomerism
- Substrate Specificity
- Torpedo
