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<p>Butyrylcholinesterase (BChE; EC 3.1.1.8), a serine hydrolase found in various tissues, hydrolyses choline esters such as acetylcholine and succinylcholine, as well as other esters such as heroin and acetylsalicylic acid. It is considered to play a role in lipid metabolism as it belongs to the same enzyme group as lipases and its catalytic subunits are similar. In this study, the effects of unsaturated fatty acids, namely arachidonic (AA), linoleic (LA), alpha-linolenic (ALA) and oleic acid (OA), on equine serum BChE (EqBChE) were investigated. Enzyme activity was measured by the modified Ellman method. When the activity results were evaluated, the IC50 values were found 45.49, 8.465, 1556, and 56.57 μM; while the Ki values were 63.92, 11.46, 1800, and 15.24 μM for AA, ALA, LA, and OA, respectively. Analysis of the kinetic results showed that ALA was compatible with mixed inhibition and other fatty acids were compatible with non-competitive inhibition, a special type of mixed inhibition. Molecular docking predicted binding of the fatty acids to the active site, as well as to predicted allosteric sites. The results of this study provide another support to the hypothesis that cholinesterases are associated with lipid metabolism.</p>

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Inhibitor Action of Unsaturated Fatty Acids on Equine Serum Butyrylcholinesterase

  • 期刊论文

  • 发表日期：

    2025年2月22日

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  • Mehmet Berk Akay,
  • Kubra Sener,
  • Suat Sari,
  • Ebru Bodur

摘要

Butyrylcholinesterase (BChE; EC 3.1.1.8), a serine hydrolase found in various tissues, hydrolyses choline esters such as acetylcholine and succinylcholine, as well as other esters such as heroin and acetylsalicylic acid. It is considered to play a role in lipid metabolism as it belongs to the same enzyme group as lipases and its catalytic subunits are similar. In this study, the effects of unsaturated fatty acids, namely arachidonic (AA), linoleic (LA), alpha-linolenic (ALA) and oleic acid (OA), on equine serum BChE (EqBChE) were investigated. Enzyme activity was measured by the modified Ellman method. When the activity results were evaluated, the IC50 values were found 45.49, 8.465, 1556, and 56.57 μM; while the Ki values were 63.92, 11.46, 1800, and 15.24 μM for AA, ALA, LA, and OA, respectively. Analysis of the kinetic results showed that ALA was compatible with mixed inhibition and other fatty acids were compatible with non-competitive inhibition, a special type of mixed inhibition. Molecular docking predicted binding of the fatty acids to the active site, as well as to predicted allosteric sites. The results of this study provide another support to the hypothesis that cholinesterases are associated with lipid metabolism.