Component

6-Hydroxymelatonin

6-Hydroxymelatonin. Species, exposure and limitations are retained in each linked claim.

5 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. Recombinant human CYP1A1 catalyzed melatonin 6-hydroxylation.

    Human cytochrome P450 1A1 → 6-Hydroxymelatonin source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"}
    experimental_model
    Recombinant P450 screen and mouse brain comparisons
    exposure
    Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation
    limitations
    Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity.
    nutrient_topic
    Melatonin research collection; topical membership is not evidence of a direct dietary effect. · Melatonin
    organism
    Human recombinant enzymes; separate mouse knockout experiment
    plain_language
    Melatonin has multiple metabolic routes whose importance depends on enzyme and tissue.
    primary_references
    [melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410
    tissue_or_cell_type
    Oxidative melatonin metabolism

    Melatonin: synthesis, receptors, circadian timing and nutrient interactions (2026-09-17) · lines 565–576

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant P450 screen and mouse brain comparisons · source_derived_draft · unverified_draft

    ### melatonin-cyp-1a1-hydroxylation Recombinant human CYP1A1 catalyzed melatonin 6-hydroxylation. Condition category: normal nutrient_topic: Melatonin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Melatonin has multiple metabolic routes whose importance depends on enzyme and tissue. organism: Human recombinant enzymes; separate mouse knockout experiment tissue_or_cell_type: Oxidative melatonin metabolism experimental_model: Recombinant P450 screen and mouse brain comparisons limitations: Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity. exposure: Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation evidence_span: {"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"} [melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410
    Complete structured claim and evidence

  2. Recombinant human CYP1B1 catalyzed melatonin 6-hydroxylation.

    Human cytochrome P450 1B1 / CYP1B1 → 6-Hydroxymelatonin source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"}
    experimental_model
    Recombinant P450 screen and mouse brain comparisons
    exposure
    Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation
    limitations
    Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity.
    nutrient_topic
    Melatonin research collection; topical membership is not evidence of a direct dietary effect. · Melatonin
    organism
    Human recombinant enzymes; separate mouse knockout experiment
    plain_language
    Melatonin has multiple metabolic routes whose importance depends on enzyme and tissue.
    primary_references
    [melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410
    tissue_or_cell_type
    Oxidative melatonin metabolism

    Melatonin: synthesis, receptors, circadian timing and nutrient interactions (2026-09-17) · lines 578–589

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant P450 screen and mouse brain comparisons · source_derived_draft · unverified_draft

    ### melatonin-cyp-1b1-hydroxylation Recombinant human CYP1B1 catalyzed melatonin 6-hydroxylation. Condition category: normal nutrient_topic: Melatonin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Melatonin has multiple metabolic routes whose importance depends on enzyme and tissue. organism: Human recombinant enzymes; separate mouse knockout experiment tissue_or_cell_type: Oxidative melatonin metabolism experimental_model: Recombinant P450 screen and mouse brain comparisons limitations: Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity. exposure: Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation evidence_span: {"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"} [melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410
    Complete structured claim and evidence

  3. Recombinant human CYP2C19 catalyzed melatonin 6-hydroxylation to a minor extent in this screen.

    Human cytochrome P450 2C19 → 6-Hydroxymelatonin source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"}
    experimental_model
    Recombinant P450 screen and mouse brain comparisons
    exposure
    Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation
    limitations
    Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity.
    nutrient_topic
    Melatonin research collection; topical membership is not evidence of a direct dietary effect. · Melatonin
    organism
    Human recombinant enzymes; separate mouse knockout experiment
    plain_language
    Melatonin has multiple metabolic routes whose importance depends on enzyme and tissue.
    primary_references
    [melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410
    tissue_or_cell_type
    Oxidative melatonin metabolism

    Melatonin: synthesis, receptors, circadian timing and nutrient interactions (2026-09-17) · lines 591–602

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant P450 screen and mouse brain comparisons · source_derived_draft · unverified_draft

    ### melatonin-cyp-2c19-hydroxylation Recombinant human CYP2C19 catalyzed melatonin 6-hydroxylation to a minor extent in this screen. Condition category: normal nutrient_topic: Melatonin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Melatonin has multiple metabolic routes whose importance depends on enzyme and tissue. organism: Human recombinant enzymes; separate mouse knockout experiment tissue_or_cell_type: Oxidative melatonin metabolism experimental_model: Recombinant P450 screen and mouse brain comparisons limitations: Catalytic capacity in an enzyme assay is not whole-body contribution. CYP1B1 is an extrahepatic route; human proteins are not substituted for mouse knockout identity. exposure: Eleven P450 isozymes; NADPH-dependent 6-hydroxylation/O-demethylation evidence_span: {"source_cache": "artifacts/melatonin-research/15616152.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2", "start_char": 0, "end_char": 1733, "text_sha256": "482334074e10503323360f236e00b5b837c5b082a7cda4df000a23d491bff8a2"} [melatonin-p15616152] Metabolism of melatonin by human cytochromes p450. (2005). https://pubmed.ncbi.nlm.nih.gov/15616152/ DOI: 10.1124/dmd.104.002410
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. CYP1A2 was the principal high-affinity, but not exclusive, enzyme for melatonin 6-hydroxylation.

    Human cytochrome P450 1A2 → Melatonin source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/dim-research/11317475.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "503f4e9d299c6c978aa1e867a32cdc7b4f5c191290b74415f0f152d3b2f0d87d", "start_char": 0, "end_char": 1580, "text_sha256": "503f4e9d299c6c978aa1e867a32cdc7b4f5c191290b74415f0f152d3b2f0d87d"}
    experimental_model
    Human microsomes, expressed enzymes and inhibition assays
    exposure
    Substrate range 1-1000 micromolar
    limitations
    In-vitro pathway identification; no DIM coadministration, sleep outcome or proof that DIM lowers nighttime melatonin.
    nutrient_topic
    Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. · 3,3'-Diindolylmethane / DIM
    organism
    Human liver CYP systems
    plain_language
    Melatonin shares the enzyme; a DIM effect on sleep cannot be read directly from this edge.
    primary_references
    [dim-p11317475] Cytochrome P450 isoforms involved in melatonin metabolism in human liver microsomes. (2001). https://pubmed.ncbi.nlm.nih.gov/11317475/ DOI: 10.1007/s002280000245
    tissue_or_cell_type
    Melatonin 6-hydroxylation

    Diindolylmethane (DIM): formation, receptor signaling, metabolism and drug interactions (2026-09-17) · lines 818–829

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human microsomes, expressed enzymes and inhibition assays · source_derived_draft · unverified_draft

    ### dim-melatonin-1a2 CYP1A2 was the principal high-affinity, but not exclusive, enzyme for melatonin 6-hydroxylation. Condition category: normal nutrient_topic: Diindolylmethane (DIM) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Melatonin shares the enzyme; a DIM effect on sleep cannot be read directly from this edge. organism: Human liver CYP systems tissue_or_cell_type: Melatonin 6-hydroxylation experimental_model: Human microsomes, expressed enzymes and inhibition assays limitations: In-vitro pathway identification; no DIM coadministration, sleep outcome or proof that DIM lowers nighttime melatonin. exposure: Substrate range 1-1000 micromolar evidence_span: {"source_cache": "artifacts/dim-research/11317475.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "503f4e9d299c6c978aa1e867a32cdc7b4f5c191290b74415f0f152d3b2f0d87d", "start_char": 0, "end_char": 1580, "text_sha256": "503f4e9d299c6c978aa1e867a32cdc7b4f5c191290b74415f0f152d3b2f0d87d"} [dim-p11317475] Cytochrome P450 isoforms involved in melatonin metabolism in human liver microsomes. (2001). https://pubmed.ncbi.nlm.nih.gov/11317475/ DOI: 10.1007/s002280000245
    Complete structured claim and evidence

  2. SULT1A1 had the strongest tested sulfating activity toward 6-hydroxymelatonin.

    Human sulfotransferase 1A1 / SULT1A1 → 6-Sulfatoxymelatonin / aMT6s source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/melatonin-research/26577053.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ab887dc7012d5f393de52ecf842b67282d51b61bac705b9ab187c1a3e24331d5", "start_char": 0, "end_char": 1378, "text_sha256": "ab887dc7012d5f393de52ecf842b67282d51b61bac705b9ab187c1a3e24331d5"}
    experimental_model
    Thirteen human SULT enzymes, labeled cells and tissue cytosols
    exposure
    6-hydroxymelatonin and N-acetylserotonin substrates; sulfate metabolic labeling
    limitations
    Enzyme ranking applies to tested conditions. Sulfation is a separate step from P450 hydroxylation; no dietary sulfur threshold was established.
    nutrient_topic
    Melatonin research collection; topical membership is not evidence of a direct dietary effect. · Melatonin
    organism
    Human recombinant enzymes, HepG2 and Caco-2 cells
    plain_language
    The hydroxylated metabolite undergoes another reaction before common urinary measurement.
    primary_references
    [melatonin-p26577053] Sulfation of 6-hydroxymelatonin, N-acetylserotonin and 4-hydroxyramelteon by the human cytosolic sulfotransferases (SULTs). (2016). https://pubmed.ncbi.nlm.nih.gov/26577053/ DOI: 10.3109/00498254.2015.1107656
    tissue_or_cell_type
    Sulfate conjugation

    Melatonin: synthesis, receptors, circadian timing and nutrient interactions (2026-09-17) · lines 630–641

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Thirteen human SULT enzymes, labeled cells and tissue cytosols · source_derived_draft · unverified_draft

    ### melatonin-sult1a1 SULT1A1 had the strongest tested sulfating activity toward 6-hydroxymelatonin. Condition category: normal nutrient_topic: Melatonin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The hydroxylated metabolite undergoes another reaction before common urinary measurement. organism: Human recombinant enzymes, HepG2 and Caco-2 cells tissue_or_cell_type: Sulfate conjugation experimental_model: Thirteen human SULT enzymes, labeled cells and tissue cytosols limitations: Enzyme ranking applies to tested conditions. Sulfation is a separate step from P450 hydroxylation; no dietary sulfur threshold was established. exposure: 6-hydroxymelatonin and N-acetylserotonin substrates; sulfate metabolic labeling evidence_span: {"source_cache": "artifacts/melatonin-research/26577053.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ab887dc7012d5f393de52ecf842b67282d51b61bac705b9ab187c1a3e24331d5", "start_char": 0, "end_char": 1378, "text_sha256": "ab887dc7012d5f393de52ecf842b67282d51b61bac705b9ab187c1a3e24331d5"} [melatonin-p26577053] Sulfation of 6-hydroxymelatonin, N-acetylserotonin and 4-hydroxyramelteon by the human cytosolic sulfotransferases (SULTs). (2016). https://pubmed.ncbi.nlm.nih.gov/26577053/ DOI: 10.3109/00498254.2015.1107656
    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