ArticleThe Biochemical journal1998
Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 84 citations in OpenAlex.
- Screening of ester-forming and hydrolyzing enzymes linked to pheromone production in Ips typographus (Linnaeus, 1758).BMC genomics · 2026Article
- Effects of dialkoxybenzenes against Varroa destructor and identification of 1-allyloxy-4-propoxybenzene as a promising acaricide candidate.Scientific reports · 2023Article
- Essential Oils for a Sustainable Control of Honeybee Varroosis.Veterinary sciences · 2023Review
- Synergistic Field Crop Pest Management Properties of Plant-Derived Essential Oils in Combination with Synthetic Pesticides and Bioactive Molecules: A Review.Foods (Basel, Switzerland) · 2021Review
- Molecular Targets for Components of Essential Oils in the Insect Nervous System-A Review.Molecules (Basel, Switzerland) · 2017Review
- Human Erythrocyte Acetylcholinesterase in Health and Disease.Molecules (Basel, Switzerland) · 2017Review
- Recombinant expression and biochemical characterization of the catalytic domain of acetylcholinesterase-1 from the African malaria mosquito, Anopheles gambiae.Insect biochemistry and molecular biology · 2009Article
- Structural insights into substrate traffic and inhibition in acetylcholinesterase.The EMBO journal · 2006Article
- Effects of soman inhibition and of structural differences on cholinesterase molecular dynamics: a neutron scattering study.Biophysical journal · 2005Article
- Acetylcholinesterase alterations reveal the fitness cost of mutations conferring insecticide resistance.BMC evolutionary biology · 2004Article
- [Thiosubstrates of different cholinesterases].Zhurnal evoliutsionnoi biokhimii i fiziologiiArticle
- Heterologous expression, purification, and biochemical characterization of a greenbug (Schizaphis graminum) acetylcholinesterase encoded by a paralogous gene (ace-1).Journal of biochemical and molecular toxicologyArticle
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In vertebrates there are two cholinesterases, with differences in catalytic behaviour with respect to substrate concentration: butyrylcholinesterase displays an increased activity at low substrate concentrations, whereas acetylcholinesterase displays inhibition by excess substrate. In two invertebrates, Drosophila melanogaster and Caenorhabditis elegans, we found cholinesterases that showed both kinetic complexities: substrate activation at low substrate concentrations followed by inhibition at higher concentrations. These triphasic kinetics can be explained by the presence of two enzymes with different kinetic behaviours or more probably by the existence of a single enzyme regulated by the substrate concentration.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.