Component

histone deacetylase activity

Independent entity for contextual scientific-audit claims; no universal nutritional effect implied.

6 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

  1. SFN-Cys inhibited HDAC activity in vitro, whereas parent sulforaphane and SFN-GSH had little or no direct effect in the comparison.

    Sulforaphane-cysteine conjugate / SFN-Cys → histone deacetylase activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"}
    experimental_model
    Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation
    exposure
    Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition
    limitations
    High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Human HEK293 and HCT116 cells
    plain_language
    A breakdown product had a different activity from the parent molecule.
    primary_references
    [sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
    tissue_or_cell_type
    Histone deacetylase activity and histone acetylation

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 567–578

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation · source_derived_draft · unverified_draft

    ### sulforaphane-cys-hdac SFN-Cys inhibited HDAC activity in vitro, whereas parent sulforaphane and SFN-GSH had little or no direct effect in the comparison. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A breakdown product had a different activity from the parent molecule. organism: Human HEK293 and HCT116 cells tissue_or_cell_type: Histone deacetylase activity and histone acetylation experimental_model: Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation limitations: High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes. exposure: Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"} [sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
    Complete structured claim and evidence

  2. SFN-NAC also inhibited HDAC activity in the in vitro comparison.

    Sulforaphane-N-acetylcysteine conjugate / SFN-NAC → histone deacetylase activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"}
    experimental_model
    Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation
    exposure
    Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition
    limitations
    High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Human HEK293 and HCT116 cells
    plain_language
    Another separately tracked conjugate affected this enzyme readout.
    primary_references
    [sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
    tissue_or_cell_type
    Histone deacetylase activity and histone acetylation

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 580–591

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation · source_derived_draft · unverified_draft

    ### sulforaphane-nac-hdac SFN-NAC also inhibited HDAC activity in the in vitro comparison. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: Another separately tracked conjugate affected this enzyme readout. organism: Human HEK293 and HCT116 cells tissue_or_cell_type: Histone deacetylase activity and histone acetylation experimental_model: Cell exposure, enzyme assays, metabolites and chromatin immunoprecipitation limitations: High-level HDAC activity was measured without establishing universal isoform inhibition; cell effects are not cancer-treatment outcomes. exposure: Parent SFN, SFN-GSH, SFN-Cys and SFN-NAC; GST inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/15313918.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e", "start_char": 0, "end_char": 1861, "text_sha256": "9478957b1513e25cb47f13d6a1aca0df542fc851d8eb4b9c6394010e90dbe83e"} [sulforaphane-p15313918] A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase. (2004). https://pubmed.ncbi.nlm.nih.gov/15313918/ DOI: 10.1158/0008-5472.can-04-1326
    Complete structured claim and evidence

  3. Acetate supplementation had no effect on histone acetyltransferase activity in brain extracts but significantly inhibited histone deacetylase activity twofold at 2 and 4 hours after treatment and decreased HDAC 2 levels at 4 hours, leading the authors to conclude that acetyl-CoA derived from acetate supplementation increases brain histone acetylation state by reducing deacetylase activity and expression.

    Glyceryl triacetate, an oral acetate precursor → histone deacetylase activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/acetate-research/21359531.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a60e30b6fa78f5fc4d9da17279ec1ecc29dd20939df5771ba26996900102014b", "start_char": 0, "end_char": 1456, "text_sha256": "a60e30b6fa78f5fc4d9da17279ec1ecc29dd20939df5771ba26996900102014b"}
    experimental_model
    Time-course Western blot analysis of brain and liver histone acetylation in rats after a single oral dose
    exposure
    A single oral dose of 6 g/kg glyceryl triacetate, an acetate precursor
    limitations
    A large single dose of a precursor, not dietary acetate. The mechanism is loss of deacetylation rather than added acetylation, and only some marks moved.
    nutrient_topic
    Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid
    organism
    Rat
    plain_language
    The marks accumulated because they were being removed more slowly, not because more were being added.
    primary_references
    [acetate-p21359531] Acetate supplementation increases brain histone acetylation and inhibits histone deacetylase activity and expression. (2011). https://pubmed.ncbi.nlm.nih.gov/21359531/ DOI: 10.1007/s11010-011-0751-3
    tissue_or_cell_type
    Brain and liver

    Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 667–678

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Time-course Western blot analysis of brain and liver histone acetylation in rats after a single oral dose · source_derived_draft · unverified_draft

    ### acetate-acetate-inhibits-hdac Acetate supplementation had no effect on histone acetyltransferase activity in brain extracts but significantly inhibited histone deacetylase activity twofold at 2 and 4 hours after treatment and decreased HDAC 2 levels at 4 hours, leading the authors to conclude that acetyl-CoA derived from acetate supplementation increases brain histone acetylation state by reducing deacetylase activity and expression. Condition category: normal nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: The marks accumulated because they were being removed more slowly, not because more were being added. organism: Rat tissue_or_cell_type: Brain and liver experimental_model: Time-course Western blot analysis of brain and liver histone acetylation in rats after a single oral dose limitations: A large single dose of a precursor, not dietary acetate. The mechanism is loss of deacetylation rather than added acetylation, and only some marks moved. exposure: A single oral dose of 6 g/kg glyceryl triacetate, an acetate precursor evidence_span: {"source_cache": "artifacts/acetate-research/21359531.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a60e30b6fa78f5fc4d9da17279ec1ecc29dd20939df5771ba26996900102014b", "start_char": 0, "end_char": 1456, "text_sha256": "a60e30b6fa78f5fc4d9da17279ec1ecc29dd20939df5771ba26996900102014b"} [acetate-p21359531] Acetate supplementation increases brain histone acetylation and inhibits histone deacetylase activity and expression. (2011). https://pubmed.ncbi.nlm.nih.gov/21359531/ DOI: 10.1007/s11010-011-0751-3
    Complete structured claim and evidence

  4. Keto-methylselenobutyrate inhibits HDAC activity in the reported enzyme/cancer-cell experiments.

    KMSB → histone deacetylase activity source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    Cancer cells and biochemical systems
    experimental_model
    Enzyme and human cancer-cell assays
    limitations
    Not interchangeable with parent compounds or proof of dietary cancer prevention.
    organism
    Homo sapiens

    Selenium: literature corrections and mechanism additions · lines 1444–1454

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Enzyme and human cancer-cell assays · secondary_verified · secondary_verified

    ## kmsb-hdac This second distinct metabolite can also inhibit tested histone-deacetylase activity. Keto-methylselenobutyrate inhibits HDAC activity in the reported enzyme/cancer-cell experiments. Organism: Homo sapiens Cell type: Cancer cells and biochemical systems Experimental model: Enzyme and human cancer-cell assays Limitations: Not interchangeable with parent compounds or proof of dietary cancer prevention. Primary reference: [α-Keto acid metabolites of organoselenium compounds inhibit histone deacetylase activity in human colon cancer cells](https://pmc.ncbi.nlm.nih.gov/articles/PMC2718078/)
    Complete structured claim and evidence

  5. Methylselenopyruvate inhibits HDAC activity in the reported enzyme/cancer-cell experiments.

    MSP → histone deacetylase activity source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    cell_type
    Cancer cells and biochemical systems
    experimental_model
    Enzyme and human cancer-cell assays
    limitations
    Not interchangeable with parent compounds or proof of dietary cancer prevention.
    organism
    Homo sapiens

    Selenium: literature corrections and mechanism additions · lines 1432–1442

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Enzyme and human cancer-cell assays · secondary_verified · secondary_verified

    ## msp-hdac This distinct metabolite can inhibit tested histone-deacetylase activity. Methylselenopyruvate inhibits HDAC activity in the reported enzyme/cancer-cell experiments. Organism: Homo sapiens Cell type: Cancer cells and biochemical systems Experimental model: Enzyme and human cancer-cell assays Limitations: Not interchangeable with parent compounds or proof of dietary cancer prevention. Primary reference: [α-Keto acid metabolites of organoselenium compounds inhibit histone deacetylase activity in human colon cancer cells](https://pmc.ncbi.nlm.nih.gov/articles/PMC2718078/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Oxygen and serum limitation increased nuclear localisation of ACSS2, and nuclear ACSS2 recaptures acetate released from histone deacetylation for recycling by histone acetyltransferases, providing evidence for limited equilibration between nuclear and cytosolic acetyl-CoA and demonstrating that ACSS2 retains acetate to maintain histone acetylation.

    Chromatin-bound nuclear acetyl-CoA synthetase 2 → Core histone lysine acetylation source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/acetate-research/28099844.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df5e8ccde04ad8a222db774f6a8b1e8838ad6a1d918ff84b667d6dde57de188", "start_char": 0, "end_char": 1134, "text_sha256": "6df5e8ccde04ad8a222db774f6a8b1e8838ad6a1d918ff84b667d6dde57de188"}
    experimental_model
    Quantitative analysis of acetate metabolism in cultured cells under oxygen and serum limitation
    exposure
    Exogenous acetate with ACSS2 and ACSS1 manipulation under oxygen and serum limitation
    limitations
    The quantitative accounting here is the important part and it is a limiting result: demand for two-carbon units far exceeds what exogenous acetate supplies. Cultured cells at a given acetate concentration, which is not a fed human.
    nutrient_topic
    Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid
    organism
    Cultured cells
    plain_language
    An enzyme sitting on the chromatin catches the acetate released when marks are removed, and puts it straight back.
    primary_references
    [acetate-p28099844] Acetate Recapturing by Nuclear Acetyl-CoA Synthetase 2 Prevents Loss of Histone Acetylation during Oxygen and Serum Limitation. (2017). https://pubmed.ncbi.nlm.nih.gov/28099844/ DOI: 10.1016/j.celrep.2016.12.055
    tissue_or_cell_type
    Nucleus and cytosol

    Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 602–613

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Quantitative analysis of acetate metabolism in cultured cells under oxygen and serum limitation · source_derived_draft · unverified_draft

    ### acetate-nuclear-acss2-recapture Oxygen and serum limitation increased nuclear localisation of ACSS2, and nuclear ACSS2 recaptures acetate released from histone deacetylation for recycling by histone acetyltransferases, providing evidence for limited equilibration between nuclear and cytosolic acetyl-CoA and demonstrating that ACSS2 retains acetate to maintain histone acetylation. Condition category: normal nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: An enzyme sitting on the chromatin catches the acetate released when marks are removed, and puts it straight back. organism: Cultured cells tissue_or_cell_type: Nucleus and cytosol experimental_model: Quantitative analysis of acetate metabolism in cultured cells under oxygen and serum limitation limitations: The quantitative accounting here is the important part and it is a limiting result: demand for two-carbon units far exceeds what exogenous acetate supplies. Cultured cells at a given acetate concentration, which is not a fed human. exposure: Exogenous acetate with ACSS2 and ACSS1 manipulation under oxygen and serum limitation evidence_span: {"source_cache": "artifacts/acetate-research/28099844.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6df5e8ccde04ad8a222db774f6a8b1e8838ad6a1d918ff84b667d6dde57de188", "start_char": 0, "end_char": 1134, "text_sha256": "6df5e8ccde04ad8a222db774f6a8b1e8838ad6a1d918ff84b667d6dde57de188"} [acetate-p28099844] Acetate Recapturing by Nuclear Acetyl-CoA Synthetase 2 Prevents Loss of Histone Acetylation during Oxygen and Serum Limitation. (2017). https://pubmed.ncbi.nlm.nih.gov/28099844/ DOI: 10.1016/j.celrep.2016.12.055
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards