Component

Human cytochrome P450 2A6 / CYP2A6

Human cytochrome P450 2A6 / CYP2A6. Species, exposure and limitations are retained in each linked claim.

16 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. Human CYP2A6 catalyzed conversion of coumarin to 7-hydroxycoumarin.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coumarin-research/15665333.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "79f42118f337ffe818b92138941685126173355131f8e12ca7cae9a437800a5b", "start_char": 0, "end_char": 1689, "text_sha256": "79f42118f337ffe818b92138941685126173355131f8e12ca7cae9a437800a5b"}
    experimental_model
    Purified human CYP2A6 kinetic experiments
    exposure
    Coumarin oxidation; stopped-flow and steady-state kinetics, selected measures at 23 C
    limitations
    Biochemical rates do not measure whole-body clearance; accessory b5 species is not specified in the abstract.
    nutrient_topic
    Coumarin research collection; topical membership is not evidence of a direct dietary effect. · Coumarin
    organism
    Human CYP2A6 with reconstituted accessory proteins
    plain_language
    CYP2A6 adds an oxygen-containing group to coumarin.
    primary_references
    [coumarin-p15665333] Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6. (2005). https://pubmed.ncbi.nlm.nih.gov/15665333/ DOI: 10.1074/jbc.m411019200
    tissue_or_cell_type
    Reconstituted enzyme system

    Coumarin: metabolism, signaling and nutrient connections (2026-09-17) · lines 137–148

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human CYP2A6 kinetic experiments · source_derived_draft · unverified_draft

    ### coumarin-2a6-7oh Human CYP2A6 catalyzed conversion of coumarin to 7-hydroxycoumarin. Condition category: normal nutrient_topic: Coumarin research collection; topical membership is not evidence of a direct dietary effect. plain_language: CYP2A6 adds an oxygen-containing group to coumarin. organism: Human CYP2A6 with reconstituted accessory proteins tissue_or_cell_type: Reconstituted enzyme system experimental_model: Purified human CYP2A6 kinetic experiments limitations: Biochemical rates do not measure whole-body clearance; accessory b5 species is not specified in the abstract. exposure: Coumarin oxidation; stopped-flow and steady-state kinetics, selected measures at 23 C evidence_span: {"source_cache": "artifacts/coumarin-research/15665333.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "79f42118f337ffe818b92138941685126173355131f8e12ca7cae9a437800a5b", "start_char": 0, "end_char": 1689, "text_sha256": "79f42118f337ffe818b92138941685126173355131f8e12ca7cae9a437800a5b"} [coumarin-p15665333] Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6. (2005). https://pubmed.ncbi.nlm.nih.gov/15665333/ DOI: 10.1074/jbc.m411019200
    Complete structured claim and evidence
  2. CYP2A6 Asn297 hydrogen bonding oriented coumarin within a compact hydrophobic active site for position-selective oxidation.

    Human cytochrome P450 2A6 / CYP2A6 → Coumarin source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coumarin-research/16086027.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "df98434feed879e206e54c520d496e9711581107f6aec58bd9dcc1c74ed5d49d", "start_char": 0, "end_char": 532, "text_sha256": "df98434feed879e206e54c520d496e9711581107f6aec58bd9dcc1c74ed5d49d"}
    experimental_model
    X-ray structures of ligand-bound human CYP2A6
    exposure
    Coumarin and methoxsalen-bound structures
    limitations
    Structure demonstrates binding geometry, not clinical effects or dietary iron responsiveness.
    nutrient_topic
    Coumarin research collection; topical membership is not evidence of a direct dietary effect. · Coumarin
    organism
    Human protein
    plain_language
    The enzyme holds coumarin in a specific orientation.
    primary_references
    [coumarin-p16086027] Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen. (2005). https://pubmed.ncbi.nlm.nih.gov/16086027/ DOI: 10.1038/nsmb971
    tissue_or_cell_type
    CYP2A6 active site

    Coumarin: metabolism, signaling and nutrient connections (2026-09-17) · lines 163–174

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray structures of ligand-bound human CYP2A6 · source_derived_draft · unverified_draft

    ### coumarin-binding-orientation CYP2A6 Asn297 hydrogen bonding oriented coumarin within a compact hydrophobic active site for position-selective oxidation. Condition category: normal nutrient_topic: Coumarin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme holds coumarin in a specific orientation. organism: Human protein tissue_or_cell_type: CYP2A6 active site experimental_model: X-ray structures of ligand-bound human CYP2A6 limitations: Structure demonstrates binding geometry, not clinical effects or dietary iron responsiveness. exposure: Coumarin and methoxsalen-bound structures evidence_span: {"source_cache": "artifacts/coumarin-research/16086027.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "df98434feed879e206e54c520d496e9711581107f6aec58bd9dcc1c74ed5d49d", "start_char": 0, "end_char": 532, "text_sha256": "df98434feed879e206e54c520d496e9711581107f6aec58bd9dcc1c74ed5d49d"} [coumarin-p16086027] Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen. (2005). https://pubmed.ncbi.nlm.nih.gov/16086027/ DOI: 10.1038/nsmb971
    Complete structured claim and evidence

What acts on it

  1. Cinnamaldehyde inhibited recombinant human CYP2A6, with reported IC50 6.1 micromolar; inhibition increased with time and required NADPH.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ceylon-research/26851241.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2", "start_char": 0, "end_char": 1591, "text_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2"}
    experimental_model
    Recombinant human CYP assays and mechanistic static modeling
    exposure
    Cinnamaldehyde, NADPH and glutathione; modeled inhibitor concentrations 0.1 and 1 micromolar
    limitations
    Enzyme inhibition and model predictions are not measured clinical drug interactions. NADPH omission is not dietary niacin deficiency.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    Human enzyme preparations; computational model
    plain_language
    The chemical interfered with a drug-metabolizing enzyme when its catalytic system was operating.
    primary_references
    [ceylon-p26851241] Inactivation of CYP2A6 by the Dietary Phenylpropanoid trans-Cinnamic Aldehyde (Cinnamaldehyde) and Estimation of Interactions with Nicotine and Letrozole. (2016). https://pubmed.ncbi.nlm.nih.gov/26851241/ DOI: 10.1124/dmd.115.067942
    tissue_or_cell_type
    CYP2A6 reaction system

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 727–738

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human CYP assays and mechanistic static modeling · source_derived_draft · unverified_draft

    ### ceylon-cyp2a6 Cinnamaldehyde inhibited recombinant human CYP2A6, with reported IC50 6.1 micromolar; inhibition increased with time and required NADPH. Condition category: normal nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: The chemical interfered with a drug-metabolizing enzyme when its catalytic system was operating. organism: Human enzyme preparations; computational model tissue_or_cell_type: CYP2A6 reaction system experimental_model: Recombinant human CYP assays and mechanistic static modeling limitations: Enzyme inhibition and model predictions are not measured clinical drug interactions. NADPH omission is not dietary niacin deficiency. exposure: Cinnamaldehyde, NADPH and glutathione; modeled inhibitor concentrations 0.1 and 1 micromolar evidence_span: {"source_cache": "artifacts/ceylon-research/26851241.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2", "start_char": 0, "end_char": 1591, "text_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2"} [ceylon-p26851241] Inactivation of CYP2A6 by the Dietary Phenylpropanoid trans-Cinnamic Aldehyde (Cinnamaldehyde) and Estimation of Interactions with Nicotine and Letrozole. (2016). https://pubmed.ncbi.nlm.nih.gov/26851241/ DOI: 10.1124/dmd.115.067942
    Complete structured claim and evidence
  2. Added glutathione modestly but significantly reduced the extent of cinnamaldehyde-dependent CYP2A6 inhibition.

    GSH → Human cytochrome P450 2A6 / CYP2A6 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ceylon-research/26851241.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2", "start_char": 0, "end_char": 1591, "text_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2"}
    experimental_model
    Recombinant human CYP assays and mechanistic static modeling
    exposure
    Cinnamaldehyde, NADPH and glutathione; modeled inhibitor concentrations 0.1 and 1 micromolar
    limitations
    Enzyme inhibition and model predictions are not measured clinical drug interactions. NADPH omission is not dietary niacin deficiency.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    Human enzyme preparations; computational model
    plain_language
    Glutathione partially buffered this enzyme effect in the assay; supplement protection was not tested.
    primary_references
    [ceylon-p26851241] Inactivation of CYP2A6 by the Dietary Phenylpropanoid trans-Cinnamic Aldehyde (Cinnamaldehyde) and Estimation of Interactions with Nicotine and Letrozole. (2016). https://pubmed.ncbi.nlm.nih.gov/26851241/ DOI: 10.1124/dmd.115.067942
    tissue_or_cell_type
    CYP2A6 reaction system

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 740–751

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human CYP assays and mechanistic static modeling · source_derived_draft · unverified_draft

    ### ceylon-gsh-cyp Added glutathione modestly but significantly reduced the extent of cinnamaldehyde-dependent CYP2A6 inhibition. Condition category: normal nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutathione partially buffered this enzyme effect in the assay; supplement protection was not tested. organism: Human enzyme preparations; computational model tissue_or_cell_type: CYP2A6 reaction system experimental_model: Recombinant human CYP assays and mechanistic static modeling limitations: Enzyme inhibition and model predictions are not measured clinical drug interactions. NADPH omission is not dietary niacin deficiency. exposure: Cinnamaldehyde, NADPH and glutathione; modeled inhibitor concentrations 0.1 and 1 micromolar evidence_span: {"source_cache": "artifacts/ceylon-research/26851241.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2", "start_char": 0, "end_char": 1591, "text_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2"} [ceylon-p26851241] Inactivation of CYP2A6 by the Dietary Phenylpropanoid trans-Cinnamic Aldehyde (Cinnamaldehyde) and Estimation of Interactions with Nicotine and Letrozole. (2016). https://pubmed.ncbi.nlm.nih.gov/26851241/ DOI: 10.1124/dmd.115.067942
    Complete structured claim and evidence
  3. Cinnamaldehyde-dependent time-dependent inhibition of CYP2A6 required NADPH in the reconstituted assay.

    NADPH → Human cytochrome P450 2A6 / CYP2A6 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/ceylon-research/26851241.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2", "start_char": 0, "end_char": 1591, "text_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2"}
    experimental_model
    Recombinant human CYP assays and mechanistic static modeling
    exposure
    Cinnamaldehyde, NADPH and glutathione; modeled inhibitor concentrations 0.1 and 1 micromolar
    limitations
    Enzyme inhibition and model predictions are not measured clinical drug interactions. NADPH omission is not dietary niacin deficiency.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    Human enzyme preparations; computational model
    plain_language
    The enzyme had to receive reducing power for this inactivation process to develop.
    primary_references
    [ceylon-p26851241] Inactivation of CYP2A6 by the Dietary Phenylpropanoid trans-Cinnamic Aldehyde (Cinnamaldehyde) and Estimation of Interactions with Nicotine and Letrozole. (2016). https://pubmed.ncbi.nlm.nih.gov/26851241/ DOI: 10.1124/dmd.115.067942
    tissue_or_cell_type
    CYP2A6 reaction system
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 753–764

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human CYP assays and mechanistic static modeling · source_derived_draft · unverified_draft

    ### ceylon-nadph-dependence Cinnamaldehyde-dependent time-dependent inhibition of CYP2A6 required NADPH in the reconstituted assay. Condition category: machinery_impairment nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme had to receive reducing power for this inactivation process to develop. organism: Human enzyme preparations; computational model tissue_or_cell_type: CYP2A6 reaction system experimental_model: Recombinant human CYP assays and mechanistic static modeling limitations: Enzyme inhibition and model predictions are not measured clinical drug interactions. NADPH omission is not dietary niacin deficiency. exposure: Cinnamaldehyde, NADPH and glutathione; modeled inhibitor concentrations 0.1 and 1 micromolar evidence_span: {"source_cache": "artifacts/ceylon-research/26851241.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2", "start_char": 0, "end_char": 1591, "text_sha256": "c2fb6b18a3ba708f060d53011ea0e198f98fe980930297e714c488a41413b5a2"} [ceylon-p26851241] Inactivation of CYP2A6 by the Dietary Phenylpropanoid trans-Cinnamic Aldehyde (Cinnamaldehyde) and Estimation of Interactions with Nicotine and Letrozole. (2016). https://pubmed.ncbi.nlm.nih.gov/26851241/ DOI: 10.1124/dmd.115.067942
    Complete structured claim and evidence
  4. Mangiferin reduced measured CYP2A6 activity in the hepatocyte experiment.

    Mangiferin → Human cytochrome P450 2A6 / CYP2A6 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/mangiferin-research/22815239.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0", "start_char": 0, "end_char": 1728, "text_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0"}
    experimental_model
    Primary human hepatocyte exposure
    exposure
    Mangiferin 50-250 micrograms/mL for 48 hours
    limitations
    High in vitro concentrations; decreased enzyme activity is not proof of human drug-level changes. Extract and isolated mangiferin are distinct.
    nutrient_topic
    Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
    organism
    Homo sapiens
    plain_language
    A drug-metabolizing enzyme was inhibited under the tested exposure.
    primary_references
    [mangiferin-p22815239] Mangifera indica L. extract and mangiferin modulate cytochrome P450 and UDP-glucuronosyltransferase enzymes in primary cultures of human hepatocytes. (2013). https://pubmed.ncbi.nlm.nih.gov/22815239/ DOI: 10.1002/ptr.4782
    tissue_or_cell_type
    Cultured hepatocytes

    Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 783–794

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Primary human hepatocyte exposure · source_derived_draft · unverified_draft

    ### mangiferin-cyp2a6-activity Mangiferin reduced measured CYP2A6 activity in the hepatocyte experiment. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A drug-metabolizing enzyme was inhibited under the tested exposure. organism: Homo sapiens tissue_or_cell_type: Cultured hepatocytes experimental_model: Primary human hepatocyte exposure limitations: High in vitro concentrations; decreased enzyme activity is not proof of human drug-level changes. Extract and isolated mangiferin are distinct. exposure: Mangiferin 50-250 micrograms/mL for 48 hours evidence_span: {"source_cache": "artifacts/mangiferin-research/22815239.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0", "start_char": 0, "end_char": 1728, "text_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0"} [mangiferin-p22815239] Mangifera indica L. extract and mangiferin modulate cytochrome P450 and UDP-glucuronosyltransferase enzymes in primary cultures of human hepatocytes. (2013). https://pubmed.ncbi.nlm.nih.gov/22815239/ DOI: 10.1002/ptr.4782
    Complete structured claim and evidence
  5. Methoxsalen filled the CYP2A6 active-site cavity without substantially changing the protein structure.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coumarin-research/16086027.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "df98434feed879e206e54c520d496e9711581107f6aec58bd9dcc1c74ed5d49d", "start_char": 0, "end_char": 532, "text_sha256": "df98434feed879e206e54c520d496e9711581107f6aec58bd9dcc1c74ed5d49d"}
    experimental_model
    X-ray structures of ligand-bound human CYP2A6
    exposure
    Coumarin and methoxsalen-bound structures
    limitations
    Structure demonstrates binding geometry, not clinical effects or dietary iron responsiveness.
    nutrient_topic
    Coumarin research collection; topical membership is not evidence of a direct dietary effect. · Coumarin
    organism
    Human protein
    plain_language
    This distinct compound fits into the same enzyme pocket.
    primary_references
    [coumarin-p16086027] Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen. (2005). https://pubmed.ncbi.nlm.nih.gov/16086027/ DOI: 10.1038/nsmb971
    tissue_or_cell_type
    CYP2A6 active site

    Coumarin: metabolism, signaling and nutrient connections (2026-09-17) · lines 176–187

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray structures of ligand-bound human CYP2A6 · source_derived_draft · unverified_draft

    ### coumarin-methoxsalen-binding Methoxsalen filled the CYP2A6 active-site cavity without substantially changing the protein structure. Condition category: normal nutrient_topic: Coumarin research collection; topical membership is not evidence of a direct dietary effect. plain_language: This distinct compound fits into the same enzyme pocket. organism: Human protein tissue_or_cell_type: CYP2A6 active site experimental_model: X-ray structures of ligand-bound human CYP2A6 limitations: Structure demonstrates binding geometry, not clinical effects or dietary iron responsiveness. exposure: Coumarin and methoxsalen-bound structures evidence_span: {"source_cache": "artifacts/coumarin-research/16086027.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "df98434feed879e206e54c520d496e9711581107f6aec58bd9dcc1c74ed5d49d", "start_char": 0, "end_char": 532, "text_sha256": "df98434feed879e206e54c520d496e9711581107f6aec58bd9dcc1c74ed5d49d"} [coumarin-p16086027] Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen. (2005). https://pubmed.ncbi.nlm.nih.gov/16086027/ DOI: 10.1038/nsmb971
    Complete structured claim and evidence
  6. Methoxsalen produced mechanism-based CYP2A6 inhibition, with reported inactivation rate 0.5/min.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coumarin-research/9143352.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dca3f4253c2977d47070bb95696634ee2e06fa9a28a3d76ac9790ce695ed6f09", "start_char": 0, "end_char": 2723, "text_sha256": "dca3f4253c2977d47070bb95696634ee2e06fa9a28a3d76ac9790ce695ed6f09"}
    experimental_model
    Human microsomal and recombinant CYP2A6 inhibitor screen
    exposure
    Coumarin 0.5–50 micromolar; 47 inhibitor/substrate probes
    limitations
    In vitro inhibition thresholds are not demonstrated clinical interactions at food exposure.
    nutrient_topic
    Coumarin research collection; topical membership is not evidence of a direct dietary effect. · Coumarin
    organism
    Human
    plain_language
    Methoxsalen can disable this enzyme during metabolism.
    primary_references
    [coumarin-p9143352] Inhibition of coumarin 7-hydroxylase activity in human liver microsomes. (1997). https://pubmed.ncbi.nlm.nih.gov/9143352/ DOI: 10.1006/abbi.1997.9964
    tissue_or_cell_type
    Liver enzyme preparations

    Coumarin: metabolism, signaling and nutrient connections (2026-09-17) · lines 553–564

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human microsomal and recombinant CYP2A6 inhibitor screen · source_derived_draft · unverified_draft

    ### coumarin-methoxsalen-inactivation Methoxsalen produced mechanism-based CYP2A6 inhibition, with reported inactivation rate 0.5/min. Condition category: normal nutrient_topic: Coumarin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Methoxsalen can disable this enzyme during metabolism. organism: Human tissue_or_cell_type: Liver enzyme preparations experimental_model: Human microsomal and recombinant CYP2A6 inhibitor screen limitations: In vitro inhibition thresholds are not demonstrated clinical interactions at food exposure. exposure: Coumarin 0.5–50 micromolar; 47 inhibitor/substrate probes evidence_span: {"source_cache": "artifacts/coumarin-research/9143352.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dca3f4253c2977d47070bb95696634ee2e06fa9a28a3d76ac9790ce695ed6f09", "start_char": 0, "end_char": 2723, "text_sha256": "dca3f4253c2977d47070bb95696634ee2e06fa9a28a3d76ac9790ce695ed6f09"} [coumarin-p9143352] Inhibition of coumarin 7-hydroxylase activity in human liver microsomes. (1997). https://pubmed.ncbi.nlm.nih.gov/9143352/ DOI: 10.1006/abbi.1997.9964
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Mass spectra indicated cinnamaldehyde-associated CYP2A6 apoprotein adduction, with reported mass addition about 132.67 Da; added glutathione did not prevent this measured adduction.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ceylon-research/32788161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4", "start_char": 0, "end_char": 2507, "text_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4"}
    experimental_model
    CYP2A6 mass spectrometry, time-dependent inhibition and numerical modeling
    exposure
    Cinnamaldehyde and separately 2-methoxycinnamaldehyde; model exposure approximately 275 mg cinnamaldehyde
    limitations
    Rat-scaled predicted human AUC is not observed AUC. Heme loss was specifically reported for the methoxy analogue; apoprotein adduction is a different endpoint from inhibition.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    Human CYP2A6; rat-scaled modeling parameters
    plain_language
    The protein acquired extra mass even with glutathione present. This differs from measuring how much enzyme activity survives.
    primary_references
    [ceylon-p32788161] Mechanisms of Herb-Drug Interactions Involving Cinnamon and CYP2A6: Focus on Time-Dependent Inhibition by Cinnamaldehyde and 2-Methoxycinnamaldehyde. (2020). https://pubmed.ncbi.nlm.nih.gov/32788161/ DOI: 10.1124/dmd.120.000087
    tissue_or_cell_type
    Enzyme apoprotein/heme; simulated drug exposure

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 766–777

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · CYP2A6 mass spectrometry, time-dependent inhibition and numerical modeling · source_derived_draft · unverified_draft

    ### ceylon-cyp-adduct Mass spectra indicated cinnamaldehyde-associated CYP2A6 apoprotein adduction, with reported mass addition about 132.67 Da; added glutathione did not prevent this measured adduction. Condition category: normal nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: The protein acquired extra mass even with glutathione present. This differs from measuring how much enzyme activity survives. organism: Human CYP2A6; rat-scaled modeling parameters tissue_or_cell_type: Enzyme apoprotein/heme; simulated drug exposure experimental_model: CYP2A6 mass spectrometry, time-dependent inhibition and numerical modeling limitations: Rat-scaled predicted human AUC is not observed AUC. Heme loss was specifically reported for the methoxy analogue; apoprotein adduction is a different endpoint from inhibition. exposure: Cinnamaldehyde and separately 2-methoxycinnamaldehyde; model exposure approximately 275 mg cinnamaldehyde evidence_span: {"source_cache": "artifacts/ceylon-research/32788161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4", "start_char": 0, "end_char": 2507, "text_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4"} [ceylon-p32788161] Mechanisms of Herb-Drug Interactions Involving Cinnamon and CYP2A6: Focus on Time-Dependent Inhibition by Cinnamaldehyde and 2-Methoxycinnamaldehyde. (2020). https://pubmed.ncbi.nlm.nih.gov/32788161/ DOI: 10.1124/dmd.120.000087
    Complete structured claim and evidence
  2. The clinical trial found no significant letrozole AUC change with the characterized C. verum regimen; the geometric mean exposure ratio was 1.11.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ceylon-research/41622703.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0d12141499aba319f8c7513f708889a4dc40fae628e26600f780be2323fe0db3", "start_char": 0, "end_char": 1643, "text_sha256": "0d12141499aba319f8c7513f708889a4dc40fae628e26600f780be2323fe0db3"}
    experimental_model
    Within-person clinical pharmacokinetic comparison
    exposure
    Characterized C. verum 2 g three times daily for five days, with day-six drug coadministration and two further cinnamon doses; nicotine gum 2 mg or letrozole 2.5 mg
    limitations
    Product- and regimen-specific short-term result, not proof of no interaction with all drugs, oils or extracts. CYP2A6 model predictions did not translate into large AUC changes here.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    Human
    plain_language
    The large interaction predicted from enzyme models was not seen for letrozole in this human study.
    primary_references
    [ceylon-p41622703] Pharmacokinetic Evaluation of a Cinnamon Product on CYP2A6 Substrate Drugs: Application of a Novel Tool Involving the Nicotine Metabolite Ratio. (2026). https://pubmed.ncbi.nlm.nih.gov/41622703/ DOI: 10.1002/cpt.70218
    tissue_or_cell_type
    16 healthy non-nicotine-using adults; plasma drug profiles

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 1208–1219

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Within-person clinical pharmacokinetic comparison · source_derived_draft · unverified_draft

    ### ceylon-letrozole-clinical The clinical trial found no significant letrozole AUC change with the characterized C. verum regimen; the geometric mean exposure ratio was 1.11. Condition category: normal nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: The large interaction predicted from enzyme models was not seen for letrozole in this human study. organism: Human tissue_or_cell_type: 16 healthy non-nicotine-using adults; plasma drug profiles experimental_model: Within-person clinical pharmacokinetic comparison limitations: Product- and regimen-specific short-term result, not proof of no interaction with all drugs, oils or extracts. CYP2A6 model predictions did not translate into large AUC changes here. exposure: Characterized C. verum 2 g three times daily for five days, with day-six drug coadministration and two further cinnamon doses; nicotine gum 2 mg or letrozole 2.5 mg evidence_span: {"source_cache": "artifacts/ceylon-research/41622703.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0d12141499aba319f8c7513f708889a4dc40fae628e26600f780be2323fe0db3", "start_char": 0, "end_char": 1643, "text_sha256": "0d12141499aba319f8c7513f708889a4dc40fae628e26600f780be2323fe0db3"} [ceylon-p41622703] Pharmacokinetic Evaluation of a Cinnamon Product on CYP2A6 Substrate Drugs: Application of a Novel Tool Involving the Nicotine Metabolite Ratio. (2026). https://pubmed.ncbi.nlm.nih.gov/41622703/ DOI: 10.1002/cpt.70218
    Complete structured claim and evidence
  3. The methoxy analogue caused reported CYP2A6 heme loss of 48.5 ± 13.4% in the LC-MS/MS experiment.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ceylon-research/32788161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4", "start_char": 0, "end_char": 2507, "text_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4"}
    experimental_model
    CYP2A6 mass spectrometry, time-dependent inhibition and numerical modeling
    exposure
    Cinnamaldehyde and separately 2-methoxycinnamaldehyde; model exposure approximately 275 mg cinnamaldehyde
    limitations
    Rat-scaled predicted human AUC is not observed AUC. Heme loss was specifically reported for the methoxy analogue; apoprotein adduction is a different endpoint from inhibition.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    Human CYP2A6; rat-scaled modeling parameters
    plain_language
    Heme damage was measured for the methoxy analogue; this number should not be attributed to cinnamaldehyde.
    primary_references
    [ceylon-p32788161] Mechanisms of Herb-Drug Interactions Involving Cinnamon and CYP2A6: Focus on Time-Dependent Inhibition by Cinnamaldehyde and 2-Methoxycinnamaldehyde. (2020). https://pubmed.ncbi.nlm.nih.gov/32788161/ DOI: 10.1124/dmd.120.000087
    tissue_or_cell_type
    Enzyme apoprotein/heme; simulated drug exposure

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 779–790

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    ### ceylon-methoxy-heme The methoxy analogue caused reported CYP2A6 heme loss of 48.5 ± 13.4% in the LC-MS/MS experiment. Condition category: normal nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: Heme damage was measured for the methoxy analogue; this number should not be attributed to cinnamaldehyde. organism: Human CYP2A6; rat-scaled modeling parameters tissue_or_cell_type: Enzyme apoprotein/heme; simulated drug exposure experimental_model: CYP2A6 mass spectrometry, time-dependent inhibition and numerical modeling limitations: Rat-scaled predicted human AUC is not observed AUC. Heme loss was specifically reported for the methoxy analogue; apoprotein adduction is a different endpoint from inhibition. exposure: Cinnamaldehyde and separately 2-methoxycinnamaldehyde; model exposure approximately 275 mg cinnamaldehyde evidence_span: {"source_cache": "artifacts/ceylon-research/32788161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4", "start_char": 0, "end_char": 2507, "text_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4"} [ceylon-p32788161] Mechanisms of Herb-Drug Interactions Involving Cinnamon and CYP2A6: Focus on Time-Dependent Inhibition by Cinnamaldehyde and 2-Methoxycinnamaldehyde. (2020). https://pubmed.ncbi.nlm.nih.gov/32788161/ DOI: 10.1124/dmd.120.000087
    Complete structured claim and evidence
  4. The clinical trial found no significant nicotine AUC change with the characterized C. verum regimen; the geometric mean exposure ratio was 0.98.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ceylon-research/41622703.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0d12141499aba319f8c7513f708889a4dc40fae628e26600f780be2323fe0db3", "start_char": 0, "end_char": 1643, "text_sha256": "0d12141499aba319f8c7513f708889a4dc40fae628e26600f780be2323fe0db3"}
    experimental_model
    Within-person clinical pharmacokinetic comparison
    exposure
    Characterized C. verum 2 g three times daily for five days, with day-six drug coadministration and two further cinnamon doses; nicotine gum 2 mg or letrozole 2.5 mg
    limitations
    Product- and regimen-specific short-term result, not proof of no interaction with all drugs, oils or extracts. CYP2A6 model predictions did not translate into large AUC changes here.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    Human
    plain_language
    The large interaction predicted from enzyme models was not seen for nicotine in this human study.
    primary_references
    [ceylon-p41622703] Pharmacokinetic Evaluation of a Cinnamon Product on CYP2A6 Substrate Drugs: Application of a Novel Tool Involving the Nicotine Metabolite Ratio. (2026). https://pubmed.ncbi.nlm.nih.gov/41622703/ DOI: 10.1002/cpt.70218
    tissue_or_cell_type
    16 healthy non-nicotine-using adults; plasma drug profiles

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 1195–1206

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Within-person clinical pharmacokinetic comparison · source_derived_draft · unverified_draft

    ### ceylon-nicotine-clinical The clinical trial found no significant nicotine AUC change with the characterized C. verum regimen; the geometric mean exposure ratio was 0.98. Condition category: normal nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: The large interaction predicted from enzyme models was not seen for nicotine in this human study. organism: Human tissue_or_cell_type: 16 healthy non-nicotine-using adults; plasma drug profiles experimental_model: Within-person clinical pharmacokinetic comparison limitations: Product- and regimen-specific short-term result, not proof of no interaction with all drugs, oils or extracts. CYP2A6 model predictions did not translate into large AUC changes here. exposure: Characterized C. verum 2 g three times daily for five days, with day-six drug coadministration and two further cinnamon doses; nicotine gum 2 mg or letrozole 2.5 mg evidence_span: {"source_cache": "artifacts/ceylon-research/41622703.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0d12141499aba319f8c7513f708889a4dc40fae628e26600f780be2323fe0db3", "start_char": 0, "end_char": 1643, "text_sha256": "0d12141499aba319f8c7513f708889a4dc40fae628e26600f780be2323fe0db3"} [ceylon-p41622703] Pharmacokinetic Evaluation of a Cinnamon Product on CYP2A6 Substrate Drugs: Application of a Novel Tool Involving the Nicotine Metabolite Ratio. (2026). https://pubmed.ncbi.nlm.nih.gov/41622703/ DOI: 10.1002/cpt.70218
    Complete structured claim and evidence
  5. The rat-scaled static model predicted a 4.92-fold letrozole AUC with the modeled cinnamaldehyde exposure.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ceylon-research/32788161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4", "start_char": 0, "end_char": 2507, "text_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4"}
    experimental_model
    CYP2A6 mass spectrometry, time-dependent inhibition and numerical modeling
    exposure
    Cinnamaldehyde and separately 2-methoxycinnamaldehyde; model exposure approximately 275 mg cinnamaldehyde
    limitations
    Rat-scaled predicted human AUC is not observed AUC. Heme loss was specifically reported for the methoxy analogue; apoprotein adduction is a different endpoint from inhibition.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    Human CYP2A6; rat-scaled modeling parameters
    plain_language
    This was a forecast from enzyme data and assumptions, not a result in people.
    primary_references
    [ceylon-p32788161] Mechanisms of Herb-Drug Interactions Involving Cinnamon and CYP2A6: Focus on Time-Dependent Inhibition by Cinnamaldehyde and 2-Methoxycinnamaldehyde. (2020). https://pubmed.ncbi.nlm.nih.gov/32788161/ DOI: 10.1124/dmd.120.000087
    tissue_or_cell_type
    Enzyme apoprotein/heme; simulated drug exposure

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 805–816

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    ### ceylon-predicted-letrozole The rat-scaled static model predicted a 4.92-fold letrozole AUC with the modeled cinnamaldehyde exposure. Condition category: normal nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: This was a forecast from enzyme data and assumptions, not a result in people. organism: Human CYP2A6; rat-scaled modeling parameters tissue_or_cell_type: Enzyme apoprotein/heme; simulated drug exposure experimental_model: CYP2A6 mass spectrometry, time-dependent inhibition and numerical modeling limitations: Rat-scaled predicted human AUC is not observed AUC. Heme loss was specifically reported for the methoxy analogue; apoprotein adduction is a different endpoint from inhibition. exposure: Cinnamaldehyde and separately 2-methoxycinnamaldehyde; model exposure approximately 275 mg cinnamaldehyde evidence_span: {"source_cache": "artifacts/ceylon-research/32788161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4", "start_char": 0, "end_char": 2507, "text_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4"} [ceylon-p32788161] Mechanisms of Herb-Drug Interactions Involving Cinnamon and CYP2A6: Focus on Time-Dependent Inhibition by Cinnamaldehyde and 2-Methoxycinnamaldehyde. (2020). https://pubmed.ncbi.nlm.nih.gov/32788161/ DOI: 10.1124/dmd.120.000087
    Complete structured claim and evidence
  6. The rat-scaled static model predicted a 4.29-fold nicotine AUC with the modeled cinnamaldehyde exposure.

    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ceylon-research/32788161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4", "start_char": 0, "end_char": 2507, "text_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4"}
    experimental_model
    CYP2A6 mass spectrometry, time-dependent inhibition and numerical modeling
    exposure
    Cinnamaldehyde and separately 2-methoxycinnamaldehyde; model exposure approximately 275 mg cinnamaldehyde
    limitations
    Rat-scaled predicted human AUC is not observed AUC. Heme loss was specifically reported for the methoxy analogue; apoprotein adduction is a different endpoint from inhibition.
    nutrient_topic
    Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. · Ceylon cinnamon / Cinnamomum verum bark preparations
    organism
    Human CYP2A6; rat-scaled modeling parameters
    plain_language
    This was a forecast from enzyme data and assumptions, not a result in people.
    primary_references
    [ceylon-p32788161] Mechanisms of Herb-Drug Interactions Involving Cinnamon and CYP2A6: Focus on Time-Dependent Inhibition by Cinnamaldehyde and 2-Methoxycinnamaldehyde. (2020). https://pubmed.ncbi.nlm.nih.gov/32788161/ DOI: 10.1124/dmd.120.000087
    tissue_or_cell_type
    Enzyme apoprotein/heme; simulated drug exposure

    Ceylon cinnamon: metabolism, signaling and nutrient connections (2026-09-17) · lines 792–803

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    ### ceylon-predicted-nicotine The rat-scaled static model predicted a 4.29-fold nicotine AUC with the modeled cinnamaldehyde exposure. Condition category: normal nutrient_topic: Ceylon cinnamon research collection; topical membership is not evidence of a direct dietary effect. plain_language: This was a forecast from enzyme data and assumptions, not a result in people. organism: Human CYP2A6; rat-scaled modeling parameters tissue_or_cell_type: Enzyme apoprotein/heme; simulated drug exposure experimental_model: CYP2A6 mass spectrometry, time-dependent inhibition and numerical modeling limitations: Rat-scaled predicted human AUC is not observed AUC. Heme loss was specifically reported for the methoxy analogue; apoprotein adduction is a different endpoint from inhibition. exposure: Cinnamaldehyde and separately 2-methoxycinnamaldehyde; model exposure approximately 275 mg cinnamaldehyde evidence_span: {"source_cache": "artifacts/ceylon-research/32788161.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4", "start_char": 0, "end_char": 2507, "text_sha256": "431169f83241cb83b84dd81d84eb1db225735677cabf33f09af8b1e22dfe64f4"} [ceylon-p32788161] Mechanisms of Herb-Drug Interactions Involving Cinnamon and CYP2A6: Focus on Time-Dependent Inhibition by Cinnamaldehyde and 2-Methoxycinnamaldehyde. (2020). https://pubmed.ncbi.nlm.nih.gov/32788161/ DOI: 10.1124/dmd.120.000087
    Complete structured claim and evidence
  7. After beer or red wine in 20 adults, urinary recovery supported tyrosol-to-hydroxytyrosol conversion, and the conversion ratio tracked CYP2A6/CYP2D6 activity score, sex and beverage matrix.

    Tyrosol → Hydroxytyrosol source_derived_draftungraded
    Experimental context and source evidence
    dose
    Red wine, IPA, blonde beer or non-alcoholic beer
    duration
    Single-dose crossover
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    evidence_scope
    literature_reviewed; model-specific source-derived curation
    experimental_model
    Twenty healthy adults in a randomized crossover trial
    limitations
    Alcohol and beverage constituents are co-exposures; the study does not justify alcohol consumption for hydroxytyrosol production.
    nutrient_topic
    Hydroxytyrosol chapter; interacting nutrients, drugs, peptides and proteins retain their experimental settings. · Hydroxytyrosol
    organism
    Twenty healthy adults in a randomized crossover trial
    plain_language
    After beer or red wine in 20 adults, urinary recovery supported tyrosol-to-hydroxytyrosol conversion, and the conversion ratio tracked CYP2A6/CYP2D6 activity score, sex and beverage matrix.
    primary_references
    Generation of the Antioxidant Hydroxytyrosol from Tyrosol Present in Beer and Red Wine in a Randomized Clinical Trial. (2019). https://pubmed.ncbi.nlm.nih.gov/31540384/ DOI: 10.3390/nu11092241
    route
    Oral beverage
    tissue
    Tyrosol and hydroxytyrosol recovery with genotype score

    Hydroxytyrosol: mechanism of action and interactions (2026-09-20) · lines 55–64

    Original AI-assisted source-specific curation with primary-study citations, model, exposure, route, duration, negative findings and limitations preserved. Not publisher full text. · supports · Twenty healthy adults in a randomized crossover trial · source_derived_draft · unverified_draft

    ## hydroxytyrosol-human-tyrosol-conversion After beer or red wine in 20 adults, urinary recovery supported tyrosol-to-hydroxytyrosol conversion, and the conversion ratio tracked CYP2A6/CYP2D6 activity score, sex and beverage matrix. Model/species: Twenty healthy adults in a randomized crossover trial Tissue/system: Tyrosol and hydroxytyrosol recovery with genotype score Exposure: Red wine, IPA, blonde beer or non-alcoholic beer Route: Oral beverage Duration: Single-dose crossover Limits: Alcohol and beverage constituents are co-exposures; the study does not justify alcohol consumption for hydroxytyrosol production. Primary reference: Generation of the Antioxidant Hydroxytyrosol from Tyrosol Present in Beer and Red Wine in a Randomized Clinical Trial. (2019). https://pubmed.ncbi.nlm.nih.gov/31540384/ DOI: 10.3390/nu11092241 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    Complete structured claim and evidence
  8. Human liver microsomes and recombinant enzymes converted tyrosol to hydroxytyrosol, with CYP2A6 and CYP2D6 supported as major contributors and CYP3A4 also active in baculosomes.

    Tyrosol → Hydroxytyrosol source_derived_draftungraded
    Experimental context and source evidence
    dose
    Tyrosol with selective CYP inhibitors or recombinant enzymes
    duration
    Enzyme incubation
    evidence_access
    Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    evidence_scope
    literature_reviewed; model-specific source-derived curation
    experimental_model
    Human liver microsomes, recombinant CYPs, genotyped livers and rat control experiments
    limitations
    Relative contribution varies by genotype and setting; this does not make every tyrosol food equivalent to hydroxytyrosol dosing.
    nutrient_topic
    Hydroxytyrosol chapter; interacting nutrients, drugs, peptides and proteins retain their experimental settings. · Hydroxytyrosol
    organism
    Human liver microsomes, recombinant CYPs, genotyped livers and rat control experiments
    plain_language
    Human liver microsomes and recombinant enzymes converted tyrosol to hydroxytyrosol, with CYP2A6 and CYP2D6 supported as major contributors and CYP3A4 also active in baculosomes.
    primary_references
    CYP2D6 and CYP2A6 biotransform dietary tyrosol into hydroxytyrosol. (2017). https://pubmed.ncbi.nlm.nih.gov/27664690/ DOI: 10.1016/j.foodchem.2016.09.026
    route
    In vitro and in vivo experimental metabolism
    tissue
    Tyrosol hydroxylation

    Hydroxytyrosol: mechanism of action and interactions (2026-09-20) · lines 44–53

    Original AI-assisted source-specific curation with primary-study citations, model, exposure, route, duration, negative findings and limitations preserved. Not publisher full text. · supports · Human liver microsomes, recombinant CYPs, genotyped livers and rat control experiments · source_derived_draft · unverified_draft

    ## hydroxytyrosol-tyrosol-cyp-conversion Human liver microsomes and recombinant enzymes converted tyrosol to hydroxytyrosol, with CYP2A6 and CYP2D6 supported as major contributors and CYP3A4 also active in baculosomes. Model/species: Human liver microsomes, recombinant CYPs, genotyped livers and rat control experiments Tissue/system: Tyrosol hydroxylation Exposure: Tyrosol with selective CYP inhibitors or recombinant enzymes Route: In vitro and in vivo experimental metabolism Duration: Enzyme incubation Limits: Relative contribution varies by genotype and setting; this does not make every tyrosol food equivalent to hydroxytyrosol dosing. Primary reference: CYP2D6 and CYP2A6 biotransform dietary tyrosol into hydroxytyrosol. (2017). https://pubmed.ncbi.nlm.nih.gov/27664690/ DOI: 10.1016/j.foodchem.2016.09.026 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.
    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