ArticleNaunyn-Schmiedeberg's archives of pharmacology2026
Expanding cholinesterase function: kinetic and structural evidence for hydrolysis of long-chain fatty-acid esters.
Article in Naunyn-Schmiedeberg's archives of pharmacology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 authors.
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Abstract
Cholinesterases (ChEs), including acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), are classically known for hydrolyzing choline esters in neurotransmission. However, their structural similarity to lipases suggests a possible capacity to act on lipid esters, implicating them in systemic lipid metabolism. The hydrolytic activity of human AChE (huAChE), purified human plasma BChE (huBChE), and equine serum BChE (EqBChE) was assayed with against three fluorescent fatty-acid esters-4-methylumbelliferyl palmitate (4-MU PA), 4-methylumbelliferyl oleate (4-MU OA), and 7-hydroxycoumarinyl arachidonate (7-HC AA) as substrate-using porcine pancreatic lipase (PPL) and human recombinant lipase (HRL) as positive controls. Kinetic parameters (Kₘ, Vₘₐₓ) were determined by Michaelis-Menten analysis. Enzyme specificity was assessed via inhibition by BW284C51 or iso-OMPA and lectin affinity assays. Molecular docking explored fatty-acid esters binding to ChE active sites. PPL and HRL hydrolyzed all substrates efficiently (Vₘₐₓ/Kₘ > 500 µU·mg⁻
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