ArticleJournal of molecular modeling2008
Characterization of a complete cycle of acetylcholinesterase catalysis by ab initio QM/MM modeling.
Article in Journal of molecular modeling, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Novel Uracil-Based Inhibitors of Acetylcholinesterase with Potency for Treating Memory Impairment in an Animal Model of Alzheimer's Disease.Molecules (Basel, Switzerland) · 2022Article
- Interaction between glyphosate pesticide and amphiphilic peptides for colorimetric analysis.Nanoscale advances · 2022Article
- Mechanism and biomass association of glucuronoyl esterase: an α/β hydrolase with potential in biomass conversion.Nature communications · 2022Article
- Article
- How is acetylcholinesterase phosphonylated by soman? An ab initio QM/MM molecular dynamics study.The journal of physical chemistry. A · 2014Article
- Molecular modeling evidence for His438 flip in the mechanism of butyrylcholinesterase hysteretic behavior.Journal of molecular neuroscience : MN · 2014Article
- Reaction pathway and free energy profiles for butyrylcholinesterase-catalyzed hydrolysis of acetylthiocholine.Biochemistry · 2012Article
- Reaction pathway and free energy profile for butyrylcholinesterase-catalyzed hydrolysis of acetylcholine.The journal of physical chemistry. B · 2011Article
- Catalytic reaction mechanism of acetylcholinesterase determined by Born-Oppenheimer ab initio QM/MM molecular dynamics simulations.The journal of physical chemistry. B · 2010Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The reaction mechanism of acetylcholine hydrolysis by acetylcholinesterase, including both acylation and deacylation stages from the enzyme-substrate (ES) to the enzyme-product (EP) molecular complexes, is examined by using an ab initio type quantum mechanical - molecular mechanical (QM/MM) approach. The density functional theory PBE0/aug-6-31+G* method for a fairly large quantum part trapped inside the native protein environment, and the AMBER force field parameters in the molecular mechanical part are employed in computations. All reaction steps, including the formation of the first tetrahedral intermediate (TI1), the acylenzyme (EA) complex, the second tetrahedral intermediate (TI2), and the EP complex, are modeled at the same theoretical level. In agreement with the experimental rate constants, the estimated activation energy barrier of the deacylation stage is slightly higher than that for the acylation phase. The critical role of the non-triad Glu202 amino acid residue in orienting lytic water molecule and in stabilizing the second tetrahedral intermediate at the deacylation stage of the enzymatic process is demonstrated.
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Registered trials
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