Cited by 1,072Cholinesterase and Neurodegenerative DiseasesPhysical Organic Chemistry and Reaction KineticsEnzyme function and inhibition

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Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states

Quinn, Daniel M.·1987·Chemical Reviews

DOI 10.1021/cr00081a005

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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAcetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition statesDaniel M. QuinnCite this: Chem. Rev. 1987, 87, 5, 955–979Publication Date (Print):October 1, 1987Publication History Published online1 May 2002Published inissue 1 October 1987https://pubs.acs.org/doi/10.1021/cr00081a005https://doi.org/10.1021/cr00081a005research-articleACS PublicationsRequest reuse permissionsArticle Views6491Altmetric-Citations884LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

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Characterization of catalytic efficiency parameters of brain cholinesterases in tropical fish
Assis, C. R. D., Linhares, A. G., Oliveira, V. D. M., et al. (2014) · Fish Physiology and Biochemistry · doi:10.1007/s10695-014-9956-1 · Cited by 15
“ChEs are described as perfect enzymes, since they hydrolyze the substrate close to the diffusion-controlled limit in the medium (Quinn 1987; Tõugu 2001; Miller and Wolfenden 2002).”
Background
Comparison of salt effects on the reactions of acetylcholinesterase with cationic and anionic inhibitors
Tõugu, V., & Kesvatera, T. (2001) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00218-1 · Cited by 15
Quantitative structure-activity relationships for the pre-steady state acetylcholinesterase inhibition by carbamates
Lin, G., Liao, W., Chan, C., et al. (2005) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.20045 · Cited by 15
m-Alkyl, α,α,α-trifluoroacetophenones: A new class of potent transition state analog inhibitors of acetylcholinesterase
Nair, H. K., & Quinn, D. M. (1993) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(01)80727-7 · Cited by 15
Self-citation
Structure-activity relationships in platelet-activating factor (PAF). 8. Tetrahydrofuran derivatives as dual PAF antagonists and acetylcholinesterase inhibitors: anti-acetylcholinesterase activity and comparative SAR
Texier, L. L., Favre, E., Ronzani, N., et al. (1996) · Journal of Lipid Mediators and Cell Signalling · doi:10.1016/0929-7855(95)00053-4 · Cited by 15
Monomeric amphiphilic forms of acetylcholinesterase appear early during brain development and may correspond to biosynthetic precursors of the amphiphilic G4 forms
Inestrosa, N. C., Moreno, R. D., & Fuentes, M.-E. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90172-4 · Cited by 15
A piezoelectric sensor with propidium as a recognition element for cholinesterases
Teller, C., Halámek, J., Makower, A. K., Fournier, D. D., Schulze, H., & Scheller, F. W. (2005) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2005.02.053 · Cited by 15
Connectivity between surface and interior in catalytic subunits of acetylcholinesterases inferred from their X‐ray structures
Radić, Z. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15802 · Cited by 14
“Each catalytic subunit of this dominantly oligomeric enzyme (Taylor, 1991) is believed to independently accelerate hydrolysis of neurotransmitter acetylcholine (ACh) by about thirteen orders of magnitude (Quinn, 1987).”
BackgroundInfluential
Exploring 2-Pyrazoline derivatives as potent antidiabetic agents and cholinesterase inhibitors: Their synthesis and molecular docking studies
Uğraş, Z., Tok, F., Çakır, C., Tuna, K., Tatar, G., Mutlu, D., Sıcak, Y., Arslan, Ş., Öztürk, M., & Koçyiğit‐Kaymakçıoğlu, B. (2024) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2024.138978 · Cited by 16
Computational Evidence for the Reactivation Process of Human Acetylcholinesterase Inhibited by Carbamates
Matos, K., da Cunha, E., Abagyan, R. A., et al. (2013) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/1386207316666131217100416 · Cited by 14
“The powerful acute toxicity of organophosphorus (OP) poisons is primarily due to the fact that they are potent AChE inhibitors, forming a covalent bond with a serine residue at the active site [16].”
Background
Metabolic fingerprinting, antioxidant characterization, and enzyme-inhibitory response of Monotheca buxifolia (Falc.) A. DC. extracts
Ali, J. S., Saleem, H., Mannan, A., et al. (2020) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-020-03093-1 · Cited by 14
“This positive association of phenolics with antioxidant activity is in accordance with previous studies showing such a trend [42].”
BackgroundResult
Exploring the effectiveness of the TSR-based protein 3-D structural comparison method for protein clustering, and structural motif identification and discovery of protein kinases, hydrolases, and SARS-CoV-2’s protein via the application of amino acid grouping
Sarkar, T., Raghavan, V. V., Chen, F., et al. (2021) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2021.107479 · Cited by 14
Artificial esterase for cooperative catalysis of ester hydrolysis at pH 7
Bose, I., Bahrami, F., & Zhao, Y. (2023) · Materials Today Chemistry · doi:10.1016/j.mtchem.2023.101576 · Cited by 14
Activation/Inhibition of Cholinesterases by Excess Substrate: Interpretation of the Phenomenological b Factor in Steady-State Rate Equation
Mukhametgalieva, A. R., Nemtarev, A. V., Sykaev, V. V., Pashirova, T. N., & Masson, P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310472 · Cited by 14
“Both ChEs also display a promiscuous activity in hydrolyzing arylacylamides [9,10].”
Background
Active-site peptides of acetylcholinesterase of Electrophorus electricus: labelling of His-440 by 1-bromo-[2-14C]pinacolone and Ser-200 by tritiated diisopropyl fluorophosphate
Salih, E., Chishti, S. B., Vicedomine, P., et al. (1994) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(94)90120-1 · Cited by 14
Use of classical and 3-D QSAR to examine the hydration state of juvenile hormone esterase inhibitors
Wheelock, C. E., Nakagawa, Y., Akamatsu, M., et al. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2003.08.023 · Cited by 14
Solvolysis process of organophosphorus compound P-[2-(dimethylamino)ethyl]-N,N-dimethylphosphonamidic fluoride with simple and α-nucleophiles: a DFT study
Kesharwani, M. K., Khan, M. A. S., Bandyopadhyay, T., et al. (2009) · Theoretical Chemistry Accounts · doi:10.1007/s00214-009-0701-2 · Cited by 14
Acetylcholinesterase Choline-Based Ionic Liquid Inhibitors: In Vitro and in Silico Molecular Docking Studies
Siopa, F., Frade, R. F. M., Diniz, A., Andrade, J. M., Nicolai, M., Meirinhos, A., Lucas, S. D., Marcelo, F., Afonso, C. A. M., & Rijo, P. M. (2018) · ACS Omega · doi:10.1021/acsomega.8b02347 · Cited by 14
The structural and biochemical impacts of monomerizing human acetylcholinesterase
Bester, S. M., Adipietro, K. A., Funk, V. L., Myslinski, J. M., Keul, N. D., Cheung, J., Wilder, P. T., Wood, Z. A., Weber, D. J., Height, J. J., et al. (2019) · Protein Science · doi:10.1002/pro.3625 · Cited by 14
“within a range of percent deviation that is less than twofold difference and as such is comparable.(3,20,21) The kcat values were determined using purified enzymes (>99%) with the enzyme concentration determined quantitatively via amino acid analyses, which is about”
Method
Reactivation of VX-Inhibited Human Acetylcholinesterase by Deprotonated Pralidoxime. A Complementary Quantum Mechanical Study
da Silva, J. A. V., Pereira, A. F., LaPlante, S. R., et al. (2020) · Biomolecules · doi:10.3390/biom10020192 · Cited by 14

Authors: Quinn, D. M.
Corresponding author: Quinn, Daniel M.
Venue: Chemical Reviews
Publisher: American Chemical Society (ACS)
Published: 1987-10-01
Volume: 87
Issue: 5
Pages: 955-979
ISSN: 0009-2665 (ISSN-L)
1520-6890
DOI: 10.1021/cr00081a005
OpenAlex: W2013132270
Cited by: 1,072
References: 0
Citations by year: 2026: 15 · 2025: 23 · 2024: 32 · 2023: 40 · 2022: 37 · 2021: 40 · 2020: 42 · 2019: 52 · 2018: 49 · 2017: 42 · 2016: 39 · 2015: 44 · 2014: 50 · 2013: 36 · 2012: 33
FWCI: 5.92
Type: journal article
Language: en
Open access: closed
Locations: Chemical Reviews (publishedVersion)
Topics: Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
Physical Sciences › Chemistry › Organic Chemistry › Physical Organic Chemistry and Reaction Kinetics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
Keywords: acetylcholinesterase, enzyme structure, reaction dynamics, enzyme catalysis, acetylcholine hydrolysis, enzyme mechanism

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Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states

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