Component

KDM1A

Independent protein record; interpretation is limited by each linked claim and its study context.

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

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 it acts on

  1. KDM1A/LSD1 oxidatively removes a methyl group from H3K4me2 through a flavin-dependent reaction.

    KDM1A → Histone H3 dimethylated at K4 source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified LSD1 enzyme / histone assays and cellular RNA interference.
    limitations
    Do not extend this specific activity to trimethyllysine or every histone site. This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.
    organism
    Human
    plain_language
    Some lysine methyl marks can be erased by a flavin enzyme.
    primary_references
    [lsd1-2004] Histone demethylation mediated by the nuclear amine oxidase homolog LSD1 (2004). https://pubmed.ncbi.nlm.nih.gov/15620353/ DOI: 10.1016/j.cell.2004.12.012
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 557–565

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified LSD1 enzyme / histone assays and cellular RNA interference. · source_derived_draft · unverified_draft

    ### kdm1a-h3k4-demethylation KDM1A/LSD1 oxidatively removes a methyl group from H3K4me2 through a flavin-dependent reaction. Plain language: Some lysine methyl marks can be erased by a flavin enzyme. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Purified LSD1 enzyme / histone assays and cellular RNA interference. limitations: Do not extend this specific activity to trimethyllysine or every histone site. This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [lsd1-2004] Histone demethylation mediated by the nuclear amine oxidase homolog LSD1 (2004). https://pubmed.ncbi.nlm.nih.gov/15620353/ DOI: 10.1016/j.cell.2004.12.012
    Complete structured claim and evidence

What acts on it

  1. One of the dihydrocapsaicin metabolites obtained from intestinal fungal biotransformation showed significant inhibitory effect on lysine-specific demethylase 1 with a half-maximal inhibitory concentration of 1.99 micromolar.

    Dihydrocapsaicin → KDM1A source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dihydrocapsaicin-research/36578383.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a36fc63af6f17ba1a551c87f5c73e288e9f468affcd39bcba5baad1ee1acf338", "start_char": 0, "end_char": 1090, "text_sha256": "a36fc63af6f17ba1a551c87f5c73e288e9f468affcd39bcba5baad1ee1acf338"}
    experimental_model
    Biotransformation of dihydrocapsaicin by four cultivated human intestinal fungal strains with NMR and HRESIMS structure determination
    exposure
    Dihydrocapsaicin incubated with cultivated human intestinal fungal strains
    limitations
    An in vitro biotransformation study with cultivated strains, not a gut community. The enzyme-inhibition result is a property of an isolated metabolite, not a demonstrated effect in an animal.
    nutrient_topic
    Dihydrocapsaicin research collection; topical membership is not evidence of a direct clinical effect, and dihydrocapsaicin is recorded separately from capsaicin. · Dihydrocapsaicin
    organism
    Human intestinal fungi
    plain_language
    One of those fungal products blocks an enzyme that edits chromatin, at a low concentration.
    primary_references
    [dhc-p36578383] Biotransformation of dihydrocapsaicin by human intestinal fungi and the inhibitory effects of metabolites against LSD1. (2022). https://pubmed.ncbi.nlm.nih.gov/36578383/ DOI: 10.1016/j.heliyon.2022.e12325
    tissue_or_cell_type
    In vitro culture

    Dihydrocapsaicin: the second capsaicinoid, the hypothermia it is used to induce, what the gut and liver do to it, and what it does without TRPV1 (2026-09-21) · lines 582–593

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Biotransformation of dihydrocapsaicin by four cultivated human intestinal fungal strains with NMR and HRESIMS structure determination · source_derived_draft · unverified_draft

    ### dhc-fungal-metabolite-inhibits-lsd1 One of the dihydrocapsaicin metabolites obtained from intestinal fungal biotransformation showed significant inhibitory effect on lysine-specific demethylase 1 with a half-maximal inhibitory concentration of 1.99 micromolar. Condition category: normal nutrient_topic: Dihydrocapsaicin research collection; topical membership is not evidence of a direct clinical effect, and dihydrocapsaicin is recorded separately from capsaicin. plain_language: One of those fungal products blocks an enzyme that edits chromatin, at a low concentration. organism: Human intestinal fungi tissue_or_cell_type: In vitro culture experimental_model: Biotransformation of dihydrocapsaicin by four cultivated human intestinal fungal strains with NMR and HRESIMS structure determination limitations: An in vitro biotransformation study with cultivated strains, not a gut community. The enzyme-inhibition result is a property of an isolated metabolite, not a demonstrated effect in an animal. exposure: Dihydrocapsaicin incubated with cultivated human intestinal fungal strains evidence_span: {"source_cache": "artifacts/dihydrocapsaicin-research/36578383.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a36fc63af6f17ba1a551c87f5c73e288e9f468affcd39bcba5baad1ee1acf338", "start_char": 0, "end_char": 1090, "text_sha256": "a36fc63af6f17ba1a551c87f5c73e288e9f468affcd39bcba5baad1ee1acf338"} [dhc-p36578383] Biotransformation of dihydrocapsaicin by human intestinal fungi and the inhibitory effects of metabolites against LSD1. (2022). https://pubmed.ncbi.nlm.nih.gov/36578383/ DOI: 10.1016/j.heliyon.2022.e12325
    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