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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
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 evidenceCYP2A6 Asn297 hydrogen bonding oriented coumarin within a compact hydrophobic active site for position-selective oxidation.
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
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 evidenceAdded glutathione modestly but significantly reduced the extent of cinnamaldehyde-dependent CYP2A6 inhibition.
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 evidenceCinnamaldehyde-dependent time-dependent inhibition of CYP2A6 required NADPH in the reconstituted assay.
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 evidenceMangiferin reduced measured CYP2A6 activity in the hepatocyte experiment.
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 evidenceMethoxsalen 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 evidenceMethoxsalen 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)
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 evidenceThe 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 evidenceThe 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
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-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 evidenceThe 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 evidenceThe 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
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-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 evidenceThe 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
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-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 evidenceAfter 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.
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 evidenceHuman liver microsomes and recombinant enzymes converted tyrosol to hydroxytyrosol, with CYP2A6 and CYP2D6 supported as major contributors and CYP3A4 also active in baculosomes.
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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.