These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Correlation between the substrate structure and the rate of acetylcholinesterase hydrolysis modeled with the combined quantum mechanical/molecular mechanical studies.
    Author: Lushchekina SV, Nemukhin AV, Morozov DI, Varfolomeev SD.
    Journal: Chem Biol Interact; 2010 Sep 06; 187(1-3):59-63. PubMed ID: 20398640.
    Abstract:
    The combined quantum mechanical-molecular mechanical (QM/MM) based computational scheme for modeling the structure-reaction rate correlations was elaborated for the hydrolysis of the set of neutral esters in the active site of acetylcholinesterase (AChE). The energy barriers of hydrolysis were estimated on the basis of the equilibrium geometry configurations of the enzyme-substrate (ES) complexes. The obtained correlation between the rate of hydrolysis and the hydrophobicity of the substrate leaving group is consistent with experimental data. The developed method can be used to predict the substrate reactivity and to interpret the specific nature of the enzyme catalysis.
    [Abstract] [Full Text] [Related] [New Search]