A Hydrophobic Binding Site in Acetylcholinesterase.
Abstract
The dissociation constants have been determined and compared for a series of reversible (noncovalent) inhibitors of eel acetylcholinesterase that are structurally related to the very potent inhibitor, 1,2,3,4-tetrahydro-9-aminoacridine (THA). It is concluded that there exists on the enzyme protein, closely adjacent to the anionic subsite, a planar, conformationally flexible, hydrophobic area whose general dimensions correspond to those of THA. It is this area, acting conjointly with the adjacent anionic subsite, which provides the attraction for THA and related inhibitors. Ultraviolet absorbance maxima and pKa values are reported for many of the compounds.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1975
- Accession Number
- ADA005014
Entities
People
- George M. Steinberg
- Jan Maddox
- Joyce Cramer
- Morton L. Mednick
- Robert Rice