Article
Site-directed mutagenesis of active site residues reveals plasticity of human butyrylcholinesterase in substrate and inhibitor interactions.
Journal of neurochemistry - 1 Feb 1994
Gnatt A, Loewenstein Y, Yaron A, Schwarz M, Soreq H
Abstract excerpt
In search of the molecular mechanisms underlying the broad substrate and inhibitor specificities of butyrylcholinesterase (BuChE), we employed site-directed mutagenesis to modify the catalytic triad residue Ser198, the acyl pocket Leu286 and adjacent Phe329 residues, and Met437 and Tyr440 located...
Topics
- Animals
- Base Sequence
- Binding Sites
- Butyrylcholinesterase
- Cholinesterase Inhibitors
- Drug Interactions
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Oligonucleotide Probes
- Oocytes
- Xenopus