ArticleMolecular metabolism2024
Acetyl-CoA synthetase (ACSS2) does not generate butyryl- and crotonyl-CoA.
Article in Molecular metabolism, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 8 citations in OpenAlex.
- Beyond acetylation: Evaluating the emerging biology of lysine acylation.Cell chemical biology · 2026Review
- Research Progress on Histone Modification Regulation Mechanisms and Breeding Applications in Plant Abiotic Stress Responses.Plants (Basel, Switzerland) · 2026Review
- Epigenetic orchestrator and drug enhancer: dual roles of butyrate in regulating post-translational modification and optimizing therapeutic delivery.Cell communication and signaling : CCS · 2025Review
- ACSS2 and metabolic diseases: from lipid metabolism to therapeutic target.Lipids in health and disease · 2025Review
- Short-chain fatty acids: key antiviral mediators of gut microbiota.Frontiers in immunology · 2025Review
- Identification of a Potential PGK1 Inhibitor with the Suppression of Breast Cancer Cells Using Virtual Screening and Molecular Docking.Pharmaceuticals (Basel, Switzerland) · 2024Article
- The mystery of crotonyl-CoA.Nature chemistry · 2024Article
- Response to letter-to-the-editor: "Acetyl-CoA synthetase (ACSS2) does not generate butyryl- and crotonyl-CoA".Molecular metabolism · 2024Article
- Letter-to-the-editor on "Acetyl-CoA synthetase (ACSS2) does not generate butyryl- and crotonyl-CoA".Molecular metabolism · 2024Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acetyl and other acyl groups from different short-chain fatty acids (SCFA) competitively modify histones at various lysine sites. To fully understand the functional significance of such histone acylation, a key epigenetic mechanism, it is crucial to characterize the cellular sources of the corresponding acyl-CoA molecules required for the lysine modification. Like acetate, SCFAs such as propionate, butyrate and crotonate are thought to be the substrates used to generate the corresponding acyl-CoAs by enzymes known as acyl-CoA synthetases. The acetyl-CoA synthetase, ACSS2, which produces acetyl-CoA from acetate in the nucleocytoplasmic compartment, has been proposed to also mediate the synthesis of acyl-CoAs such as butyryl- and crotonyl-CoA from the corresponding SCFAs. This idea is now widely accepted and is sparking new research projects. However, based on our direct in vitro experiments with purified or recombinant enzymes and structural considerations, we demonstrate that ACSS2 is unable to mediate the generation of non-acetyl acyl-CoAs like butyryl- and crotonyl-CoA. It is therefore essential to re-examine published data and corresponding discussions in the light of this new finding.
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Registered trials
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