ArticleCell reports2017
Non-enzymatic N-acetylation of Lysine Residues by AcetylCoA Often Occurs via a Proximal S-acetylated Thiol Intermediate Sensitive to Glyoxalase II.
Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
68 citing papers in PubMed, 115 citations in OpenAlex.
- Crosstalk between cysteine and lysine modifications: Integrating redox and metabolic regulation.Redox biology · 2026Review
- Post-translational protein lactylation modification in lung cancer: an emerging targeted therapeutic strategy.Frontiers in immunology · 2026Review
- Cysteine S-acetylation is a widespread post-translational modification on metabolic proteins.npj metabolic health and disease · 2025Article
- Reactivity-based metabolomics reveal cysteine has glyoxalase 1-like and glyoxalase 2-like activities.Nature chemical biology · 2025Article
- Role of Histone Lactylation in Neurological Disorders.International journal of molecular sciences · 2025Review
- Lactylation: A New Metabolic Signature of Sepsis-Related Cardiac Dysfunction.Circulation research · 2025Article
- Correlations between gut microbiota and serum metabolomics in patients with neurogenic rosacea.BMC microbiology · 2025Article
- Protein post-translational modifications in serine synthetic pathway: functions and molecular mechanisms.Cell communication and signaling : CCS · 2025Review
- Lactylation and human disease.Expert reviews in molecular medicine · 2025Review
- Acetylation of proximal cysteine-lysine pairs by alcohol metabolism.Redox biology · 2025Article
- Nonenzymatic lysine D-lactylation induced by glyoxalase II substrate SLG dampens inflammatory immune responses.Cell research · 2025Article
- Overexpression of Glyoxalase 2 in Human Breast Cancer Cells: Implications for Cell Proliferation and Doxorubicin Resistance.International journal of molecular sciences · 2024Article
- Immunometabolic Maladaptations to the Tumor Microenvironment.Cold Spring Harbor perspectives in medicine · 2024Review
- Deacetylation mimetic mutation of mitochondrial SOD2 attenuates ANG II-induced hypertension by protecting against oxidative stress and inflammation.American journal of physiology. Heart and circulatory physiology · 2024Article
- Thiol-Mediated Enhancement of NACS chemical biology · 2024Article
- Review
- Post-translational protein lactylation modification in health and diseases: a double-edged sword.Journal of translational medicine · 2024Review
- Fatty acid synthesis suppresses dietary polyunsaturated fatty acid use.Nature communications · 2024Article
- COX17 acetylation via MOF-KANSL complex promotes mitochondrial integrity and function.Nature metabolism · 2023Article
- Survey of Acetylation for Thermoanaerobacter tengcongensis.Applied biochemistry and biotechnology · 2023Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Acetyl coenzyme A (AcCoA), a key intermediate in mitochondrial metabolism, N-acetylates lysine residues, disrupting and, in some cases, regulating protein function. The mitochondrial lysine deacetylase Sirtuin 3 (Sirt3) reverses this modification with benefits reported in diabetes, obesity, and aging. We show that non-enzymatic lysine N-acetylation by AcCoA is greatly enhanced by initial acetylation of a cysteine residue, followed by SN-transfer of the acetyl moiety to a nearby lysine on mitochondrial proteins and synthetic peptides. The frequent occurrence of an S-acetyl intermediate before lysine N-acetylation suggests that proximity to a thioester is a key determinant of lysine susceptibility to acetylation. The thioesterase glyoxalase II (Glo2) can limit protein S-acetylation, thereby preventing subsequent lysine N-acetylation. This suggests that the hitherto obscure role of Glo2 in mitochondria is to act upstream of Sirt3 in minimizing protein N-acetylation, thus limiting protein dysfunction when AcCoA accumulates.
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Registered trials
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.