, volume 52 , issue 3 , pages 434-445

Molecular modeling evidence for His438 flip in the mechanism of butyrylcholinesterase hysteretic behavior

Sofya V. Lushchekina ¹

Alexander V Nemukhin ^{1, 2}

Sergei D. VARFOLOMEEV ^{1, 2}

Patrick Masson ^{3, 4}

Hide authors affiliations Show authors affiliations: 4 affiliations

Computer Modeling of Biomolecular Systems Lab, N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia |

Chemistry department, M.V. Lomonosov Moscow State University, Moscow, Russia |

Eppley Institute, University of Nebraska Medical Center, Omaha, USA |

⁴

DYNAMOP, Institut de Biologie Structurale, Grenoble, France |

Publication type: Journal Article

Publication date: 2013-12-06

Springer Nature

Journal of Molecular Neuroscience

scimago Q1

wos Q3

SJR: 1.019

CiteScore: 7.0

Impact factor: 2.7

ISSN: 08958696, 15591166

DOI: 10.1007/s12031-013-0178-2

Copy DOI

PubMed ID: 24310732

General Medicine

Cellular and Molecular Neuroscience

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.

Found

1 citation

Kulakova Anna

PhD in Physics and Mathematics

37 publications, 131 citations

h-index: 6

Lomonosov Moscow State University

Research interests

Molecular modeling

Reaction mechanisms

Top-30

Journals

	1 2 3
Chemico-Biological Interactions	Chemico-Biological Interactions, 3, 18.75% Chemico-Biological Interactions 3 publications, 18.75%
Russian Chemical Bulletin	Russian Chemical Bulletin, 1, 6.25% Russian Chemical Bulletin 1 publication, 6.25%
Biomolecules	Biomolecules, 1, 6.25% Biomolecules 1 publication, 6.25%
Frontiers in Chemistry	Frontiers in Chemistry, 1, 6.25% Frontiers in Chemistry 1 publication, 6.25%
Theoretical Chemistry Accounts	Theoretical Chemistry Accounts, 1, 6.25% Theoretical Chemistry Accounts 1 publication, 6.25%
Journal of Molecular Neuroscience	Journal of Molecular Neuroscience, 1, 6.25% Journal of Molecular Neuroscience 1 publication, 6.25%
PLoS ONE	PLoS ONE, 1, 6.25% PLoS ONE 1 publication, 6.25%
Archives of Biochemistry and Biophysics	Archives of Biochemistry and Biophysics, 1, 6.25% Archives of Biochemistry and Biophysics 1 publication, 6.25%
Neuropharmacology	Neuropharmacology, 1, 6.25% Neuropharmacology 1 publication, 6.25%
Biochemical Pharmacology	Biochemical Pharmacology, 1, 6.25% Biochemical Pharmacology 1 publication, 6.25%
Industrial & Engineering Chemistry Research	Industrial & Engineering Chemistry Research, 1, 6.25% Industrial & Engineering Chemistry Research 1 publication, 6.25%
Physical Chemistry Chemical Physics	Physical Chemistry Chemical Physics, 1, 6.25% Physical Chemistry Chemical Physics 1 publication, 6.25%
Molecules	Molecules, 1, 6.25% Molecules 1 publication, 6.25%
South African Journal of Botany	South African Journal of Botany, 1, 6.25% South African Journal of Botany 1 publication, 6.25%
	1 2 3

Publishers

	1 2 3 4 5 6 7
Elsevier	Elsevier, 7, 43.75% Elsevier 7 publications, 43.75%
Springer Nature	Springer Nature, 3, 18.75% Springer Nature 3 publications, 18.75%
MDPI	MDPI, 2, 12.5% MDPI 2 publications, 12.5%
Frontiers Media S.A.	Frontiers Media S.A., 1, 6.25% Frontiers Media S.A. 1 publication, 6.25%
Public Library of Science (PLoS)	Public Library of Science (PLoS), 1, 6.25% Public Library of Science (PLoS) 1 publication, 6.25%
American Chemical Society (ACS)	American Chemical Society (ACS), 1, 6.25% American Chemical Society (ACS) 1 publication, 6.25%
Royal Society of Chemistry (RSC)	Royal Society of Chemistry (RSC), 1, 6.25% Royal Society of Chemistry (RSC) 1 publication, 6.25%
	1 2 3 4 5 6 7

We do not take into account publications without a DOI.
Statistics recalculated weekly.

Are you a researcher?

Create a profile to get free access to personal recommendations for colleagues and new articles.

Metrics

Cite this

GOST |

Cite this

GOST Copy

Lushchekina S. V. et al. Molecular modeling evidence for His438 flip in the mechanism of butyrylcholinesterase hysteretic behavior // Journal of Molecular Neuroscience. 2013. Vol. 52. No. 3. pp. 434-445.

GOST all authors (up to 50) Copy

Lushchekina S. V., Nemukhin A. V., VARFOLOMEEV S. D., Masson P. Molecular modeling evidence for His438 flip in the mechanism of butyrylcholinesterase hysteretic behavior // Journal of Molecular Neuroscience. 2013. Vol. 52. No. 3. pp. 434-445.

RIS |

Cite this

RIS Copy

TY - JOUR

DO - 10.1007/s12031-013-0178-2

UR - https://doi.org/10.1007/s12031-013-0178-2

TI - Molecular modeling evidence for His438 flip in the mechanism of butyrylcholinesterase hysteretic behavior

T2 - Journal of Molecular Neuroscience

AU - Lushchekina, Sofya V.

AU - Nemukhin, Alexander V

AU - VARFOLOMEEV, Sergei D.

AU - Masson, Patrick

PY - 2013

DA - 2013/12/06

PB - Springer Nature

SP - 434-445

IS - 3

VL - 52

PMID - 24310732

SN - 0895-8696

SN - 1559-1166

ER -

BibTex |

Cite this

BibTex (up to 50 authors) Copy

@article{2013_Lushchekina,

author = {Sofya V. Lushchekina and Alexander V Nemukhin and Sergei D. VARFOLOMEEV and Patrick Masson},

title = {Molecular modeling evidence for His438 flip in the mechanism of butyrylcholinesterase hysteretic behavior},

journal = {Journal of Molecular Neuroscience},

year = {2013},

volume = {52},

publisher = {Springer Nature},

month = {dec},

url = {https://doi.org/10.1007/s12031-013-0178-2},

number = {3},

pages = {434--445},

doi = {10.1007/s12031-013-0178-2}

}

MLA

Cite this

MLA Copy

Lushchekina, Sofya V., et al. “Molecular modeling evidence for His438 flip in the mechanism of butyrylcholinesterase hysteretic behavior.” Journal of Molecular Neuroscience, vol. 52, no. 3, Dec. 2013, pp. 434-445. https://doi.org/10.1007/s12031-013-0178-2.