ArticleJournal of molecular neuroscience : MN2014
Molecular modeling evidence for His438 flip in the mechanism of butyrylcholinesterase hysteretic behavior.
Article in Journal of molecular neuroscience : MN, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Design, synthesis, and multitarget evaluation of thiosemicarbazone-sulfonamide hybrids as potent cholinesterase and MAO-A inhibitors with neuroblastoma-associated cytotoxicity.Scientific reports · 2026Article
- Pre-Steady-State and Steady-State Kinetic Analysis of Butyrylcholinesterase-Catalyzed Hydrolysis of Mirabegron, an Arylacylamide Drug.Molecules (Basel, Switzerland) · 2024Article
- A Comprehensive Review of Cholinesterase Modeling and Simulation.Biomolecules · 2021Review
- Journal of molecular neuroscience: impacting our brains.Journal of molecular neuroscience : MN · 2014Article
- Article
- Development of organophosphate hydrolase activity in a bacterial homolog of human cholinesterase.Frontiers in chemistry · 2014Article
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Authors and funding
4 authors.
Funding
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Abstract
Cholinesterases display a hysteretic behavior with certain substrates and irreversible inhibitors. For years, this behavior has remained puzzling. However, several lines of evidence indicated that it is caused by perturbation of the catalytic triad and its water environment. In the present study, using molecular dynamics simulations of Ala328Cys BuChE mutant and wild-type BuChE in the absence and presence of a co-solvent (sucrose, glycerol), we provide evidence that hysteresis originates in a flip of the catalytic triad histidine (His438). This event is controlled by water molecules that interact with active site residues. The physiological significance of this phenomenon is still an issue.
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