Component

UDP-glucuronic acid

UDP-glucuronic acid. Species, exposure and limitations are retained in each linked claim.

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

Read recorded mechanisms Open recursive mind map

How nutrients influence it

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

How nutrients reach it in more than one step

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

Tracing routes…

What it does

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

Recorded relationships

Where it participates (unsigned role)

  1. Recombinant human UGT1A1 efficiently glucuronidated luteolin in the isoenzyme comparison.

    Human UDP-glucuronosyltransferase 1A1 / UGT1A1 → Luteolin / 3′,4′,5,7-tetrahydroxyflavone source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human recombinant UGT comparison and microsomes.
    limitations
    Relative activity depends on tissue and conjugation position. Not a claim of equal in-vivo contribution.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    A specific enzyme can attach a glucuronide group.
    primary_references
    Regioselectivity of phase II metabolism of luteolin and quercetin by UDP-glucuronosyl transferases. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12018987/ · DOI 10.1021/tx0101705

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 28–34

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant UGT comparison and microsomes. · source_derived_draft · unverified_draft

    ## luteolin-ugt1a1-formation A specific enzyme can attach a glucuronide group. Recombinant human UGT1A1 efficiently glucuronidated luteolin in the isoenzyme comparison. Model: Human recombinant UGT comparison and microsomes. Limitations: Relative activity depends on tissue and conjugation position. Not a claim of equal in-vivo contribution. Evidence access: Primary abstract Regioselectivity of phase II metabolism of luteolin and quercetin by UDP-glucuronosyl transferases. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12018987/ · DOI 10.1021/tx0101705
    Complete structured claim and evidence

  2. Recombinant human UGT1A8 efficiently glucuronidated luteolin in the isoenzyme comparison.

    Human UGT1A8 → Luteolin / 3′,4′,5,7-tetrahydroxyflavone source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human recombinant UGT comparison and microsomes.
    limitations
    Relative activity depends on tissue and conjugation position. Not a claim of equal in-vivo contribution.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    A specific enzyme can attach a glucuronide group.
    primary_references
    Regioselectivity of phase II metabolism of luteolin and quercetin by UDP-glucuronosyl transferases. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12018987/ · DOI 10.1021/tx0101705

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 36–42

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant UGT comparison and microsomes. · source_derived_draft · unverified_draft

    ## luteolin-ugt1a8-formation A specific enzyme can attach a glucuronide group. Recombinant human UGT1A8 efficiently glucuronidated luteolin in the isoenzyme comparison. Model: Human recombinant UGT comparison and microsomes. Limitations: Relative activity depends on tissue and conjugation position. Not a claim of equal in-vivo contribution. Evidence access: Primary abstract Regioselectivity of phase II metabolism of luteolin and quercetin by UDP-glucuronosyl transferases. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12018987/ · DOI 10.1021/tx0101705
    Complete structured claim and evidence

  3. Human UGT1A9 formed Luteolin 3′,4′-diglucuronide in the luteolin-conjugation study.

    Human UDP-glucuronosyltransferase 1A9 / UGT1A9 → Luteolin 3′,4′-diglucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant enzymes and UGT1A9-expressing HeLa cells.
    limitations
    Engineered expression; not a human organ concentration.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    The conjugation position defines a distinct product.
    primary_references
    Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 76–82

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant enzymes and UGT1A9-expressing HeLa cells. · source_derived_draft · unverified_draft

    ## luteolin-ugt1a9-34g The conjugation position defines a distinct product. Human UGT1A9 formed Luteolin 3′,4′-diglucuronide in the luteolin-conjugation study. Model: Recombinant enzymes and UGT1A9-expressing HeLa cells. Limitations: Engineered expression; not a human organ concentration. Evidence access: Primary abstract Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0
    Complete structured claim and evidence

  4. Human UGT1A9 formed Luteolin 3′-O-glucuronide in the luteolin-conjugation study.

    Human UDP-glucuronosyltransferase 1A9 / UGT1A9 → Luteolin 3′-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant enzymes and UGT1A9-expressing HeLa cells.
    limitations
    Engineered expression; not a human organ concentration.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    The conjugation position defines a distinct product.
    primary_references
    Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 52–58

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant enzymes and UGT1A9-expressing HeLa cells. · source_derived_draft · unverified_draft

    ## luteolin-ugt1a9-3g The conjugation position defines a distinct product. Human UGT1A9 formed Luteolin 3′-O-glucuronide in the luteolin-conjugation study. Model: Recombinant enzymes and UGT1A9-expressing HeLa cells. Limitations: Engineered expression; not a human organ concentration. Evidence access: Primary abstract Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0
    Complete structured claim and evidence

  5. Human UGT1A9 formed Luteolin 4′-O-glucuronide in the luteolin-conjugation study.

    Human UDP-glucuronosyltransferase 1A9 / UGT1A9 → Luteolin 4′-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant enzymes and UGT1A9-expressing HeLa cells.
    limitations
    Engineered expression; not a human organ concentration.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    The conjugation position defines a distinct product.
    primary_references
    Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 60–66

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant enzymes and UGT1A9-expressing HeLa cells. · source_derived_draft · unverified_draft

    ## luteolin-ugt1a9-4g The conjugation position defines a distinct product. Human UGT1A9 formed Luteolin 4′-O-glucuronide in the luteolin-conjugation study. Model: Recombinant enzymes and UGT1A9-expressing HeLa cells. Limitations: Engineered expression; not a human organ concentration. Evidence access: Primary abstract Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0
    Complete structured claim and evidence

  6. Human UGT1A9 formed Luteolin 7-O-glucuronide in the luteolin-conjugation study.

    Human UDP-glucuronosyltransferase 1A9 / UGT1A9 → Luteolin 7-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant enzymes and UGT1A9-expressing HeLa cells.
    limitations
    Engineered expression; not a human organ concentration.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    The conjugation position defines a distinct product.
    primary_references
    Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 68–74

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant enzymes and UGT1A9-expressing HeLa cells. · source_derived_draft · unverified_draft

    ## luteolin-ugt1a9-7g The conjugation position defines a distinct product. Human UGT1A9 formed Luteolin 7-O-glucuronide in the luteolin-conjugation study. Model: Recombinant enzymes and UGT1A9-expressing HeLa cells. Limitations: Engineered expression; not a human organ concentration. Evidence access: Primary abstract Breast cancer resistance protein-mediated efflux of luteolin glucuronides in HeLa cells overexpressing UDP-glucuronosyltransferase 1A9. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24092055/ · DOI 10.1007/s11095-013-1207-0
    Complete structured claim and evidence

  7. Recombinant human UGT1A9 efficiently glucuronidated luteolin in the isoenzyme comparison.

    Human UDP-glucuronosyltransferase 1A9 / UGT1A9 → Luteolin / 3′,4′,5,7-tetrahydroxyflavone source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human recombinant UGT comparison and microsomes.
    limitations
    Relative activity depends on tissue and conjugation position. Not a claim of equal in-vivo contribution.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    A specific enzyme can attach a glucuronide group.
    primary_references
    Regioselectivity of phase II metabolism of luteolin and quercetin by UDP-glucuronosyl transferases. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12018987/ · DOI 10.1021/tx0101705

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 44–50

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human recombinant UGT comparison and microsomes. · source_derived_draft · unverified_draft

    ## luteolin-ugt1a9-formation A specific enzyme can attach a glucuronide group. Recombinant human UGT1A9 efficiently glucuronidated luteolin in the isoenzyme comparison. Model: Human recombinant UGT comparison and microsomes. Limitations: Relative activity depends on tissue and conjugation position. Not a claim of equal in-vivo contribution. Evidence access: Primary abstract Regioselectivity of phase II metabolism of luteolin and quercetin by UDP-glucuronosyl transferases. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12018987/ · DOI 10.1021/tx0101705
    Complete structured claim and evidence

  8. Human UGT1A1 predominantly formed the 3-O glucuronide of trans-resveratrol in microsomal/recombinant experiments; reported Km was 149 micromolar.

    Human UDP-glucuronosyltransferase 1A1 / UGT1A1 → Resveratrol 3-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human liver/intestine microsomes and recombinant UGTs.
    limitations
    Predominant contribution is not exclusive specificity; Km is not a human plasma target.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    An independently named enzyme produces an independently named metabolite.
    primary_references
    Glucuronidation of trans-resveratrol by human liver and intestinal microsomes and UGT isoforms. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16597364/ · DOI 10.1211/jpp.58.4.0006

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 30–36

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human liver/intestine microsomes and recombinant UGTs. · source_derived_draft · unverified_draft

    ## resveratrol-ugt1a1 An independently named enzyme produces an independently named metabolite. Human UGT1A1 predominantly formed the 3-O glucuronide of trans-resveratrol in microsomal/recombinant experiments; reported Km was 149 micromolar. Model: Human liver/intestine microsomes and recombinant UGTs. Limitations: Predominant contribution is not exclusive specificity; Km is not a human plasma target. Evidence access: Primary abstract Glucuronidation of trans-resveratrol by human liver and intestinal microsomes and UGT isoforms. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16597364/ · DOI 10.1211/jpp.58.4.0006
    Complete structured claim and evidence

  9. Human UGT1A9 predominantly formed the 4′-O glucuronide of trans-resveratrol in microsomal/recombinant experiments; reported Km was 365 micromolar.

    Human UDP-glucuronosyltransferase 1A9 / UGT1A9 → Resveratrol 4′-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human liver/intestine microsomes and recombinant UGTs.
    limitations
    Predominant contribution is not exclusive specificity; Km is not a human plasma target.
    nutrient_topic
    Resveratrol collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Resveratrol
    plain_language
    An independently named enzyme produces an independently named metabolite.
    primary_references
    Glucuronidation of trans-resveratrol by human liver and intestinal microsomes and UGT isoforms. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16597364/ · DOI 10.1211/jpp.58.4.0006

    Resveratrol: metabolites, target selectivity and cross-nutrient mechanisms (2026-09-19) · lines 38–44

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human liver/intestine microsomes and recombinant UGTs. · source_derived_draft · unverified_draft

    ## resveratrol-ugt1a9 An independently named enzyme produces an independently named metabolite. Human UGT1A9 predominantly formed the 4′-O glucuronide of trans-resveratrol in microsomal/recombinant experiments; reported Km was 365 micromolar. Model: Human liver/intestine microsomes and recombinant UGTs. Limitations: Predominant contribution is not exclusive specificity; Km is not a human plasma target. Evidence access: Primary abstract Glucuronidation of trans-resveratrol by human liver and intestinal microsomes and UGT isoforms. · 2006 · https://pubmed.ncbi.nlm.nih.gov/16597364/ · DOI 10.1211/jpp.58.4.0006
    Complete structured claim and evidence

  10. UGT1A3 contributed alongside UGT2B7 to steviol glucuronidation at high substrate concentration.

    Human UDP-glucuronosyltransferase 1A3 / UGT1A3 → Steviol source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human enzyme screening and microsomal kinetics.
    limitations
    High versus low assay concentration must not be converted into an unmeasured dietary threshold.
    nutrient_topic
    Stevia collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Stevia
    plain_language
    The participating enzyme mix changes with substrate concentration.
    primary_references
    Steviol glucuronidation and its potential interaction with UDP-glucuronosyltransferase 2B7 substrates. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24296138/ · DOI 10.1016/j.fct.2013.11.028

    Stevia: glycoside metabolism, taste, ion channels and cross-nutrient mechanisms (2026-09-19) · lines 58–64

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human enzyme screening and microsomal kinetics. · source_derived_draft · unverified_draft

    ## stevia-ugt1a3 The participating enzyme mix changes with substrate concentration. UGT1A3 contributed alongside UGT2B7 to steviol glucuronidation at high substrate concentration. Model: Recombinant human enzyme screening and microsomal kinetics. Limitations: High versus low assay concentration must not be converted into an unmeasured dietary threshold. Evidence access: Primary abstract Steviol glucuronidation and its potential interaction with UDP-glucuronosyltransferase 2B7 substrates. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24296138/ · DOI 10.1016/j.fct.2013.11.028
    Complete structured claim and evidence

  11. Recombinant enzyme and microsomal assays identified UGT2B7 as the main contributor to steviol glucuronidation at low substrate concentration.

    Human UDP-glucuronosyltransferase 2B7 / UGT2B7 → Steviol source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human and rat microsomes with recombinant human UGT assays.
    limitations
    Organ-specific clearance differed; in vitro enzyme contribution is not a measured whole-body clearance fraction.
    nutrient_topic
    Stevia collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Stevia
    plain_language
    A liver clearance enzyme changes the circulating chemical form.
    primary_references
    Steviol glucuronidation and its potential interaction with UDP-glucuronosyltransferase 2B7 substrates. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24296138/ · DOI 10.1016/j.fct.2013.11.028

    Stevia: glycoside metabolism, taste, ion channels and cross-nutrient mechanisms (2026-09-19) · lines 50–56

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human and rat microsomes with recombinant human UGT assays. · source_derived_draft · unverified_draft

    ## stevia-ugt2b7 A liver clearance enzyme changes the circulating chemical form. Recombinant enzyme and microsomal assays identified UGT2B7 as the main contributor to steviol glucuronidation at low substrate concentration. Model: Human and rat microsomes with recombinant human UGT assays. Limitations: Organ-specific clearance differed; in vitro enzyme contribution is not a measured whole-body clearance fraction. Evidence access: Primary abstract Steviol glucuronidation and its potential interaction with UDP-glucuronosyltransferase 2B7 substrates. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24296138/ · DOI 10.1016/j.fct.2013.11.028
    Complete structured claim and evidence

  12. The mouse disposition study detected a fisetin glucuronide and a glucuronide of geraldol.

    Fisetin → Fisetin glucuronides, unresolved positional pool source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Mouse plasma metabolite identification after intraperitoneal dosing.
    limitations
    Positional conjugate identities remain unresolved here.
    nutrient_topic
    Fisetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Fisetin
    plain_language
    Further conjugation changes both the parent and metabolite.
    primary_references
    Fisetin disposition and metabolism in mice: Identification of geraldol as an active metabolite. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21840301/ · DOI 10.1016/j.bcp.2011.07.097

    Fisetin: metabolism, cell-state responses and cross-nutrient mechanisms (2026-09-19) · lines 32–38

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Mouse plasma metabolite identification after intraperitoneal dosing. · source_derived_draft · unverified_draft

    ## fisetin-mouse-conjugates Further conjugation changes both the parent and metabolite. The mouse disposition study detected a fisetin glucuronide and a glucuronide of geraldol. Model: Mouse plasma metabolite identification after intraperitoneal dosing. Limitations: Positional conjugate identities remain unresolved here. Evidence access: Primary abstract Fisetin disposition and metabolism in mice: Identification of geraldol as an active metabolite. · 2011 · https://pubmed.ncbi.nlm.nih.gov/21840301/ · DOI 10.1016/j.bcp.2011.07.097
    Complete structured claim and evidence

  13. Bovine liver UGT preparation converted 7-hydroxycoumarin and UDP-glucuronic acid into its glucuronide.

    Bovine liver UDP-glucuronosyltransferase preparation; isoforms unresolved → 7-Hydroxycoumarin glucuronide source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/coumarin-research/8877866.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8092618f6e2773ad94670c810fb44af7c2acedc0680674872af23af8bc55e26d", "start_char": 0, "end_char": 2114, "text_sha256": "8092618f6e2773ad94670c810fb44af7c2acedc0680674872af23af8bc55e26d"}
    experimental_model
    Enzyme assay and HPLC metabolite identification
    exposure
    7-Hydroxycoumarin plus UDP-glucuronic acid
    limitations
    Bovine preparation does not identify a dominant human UGT isoform.
    nutrient_topic
    Coumarin research collection; topical membership is not evidence of a direct dietary effect. · Coumarin
    organism
    Bovine
    plain_language
    A sugar-acid donor enables the conjugation step.
    primary_references
    [coumarin-p8877866] Analysis of the glucuronidation of 7-hydroxycoumarin by HPLC. (1996). https://pubmed.ncbi.nlm.nih.gov/8877866/ DOI: 10.1016/0731-7085(96)01801-8
    tissue_or_cell_type
    Liver homogenate/crude UGT preparation

    Coumarin: metabolism, signaling and nutrient connections (2026-09-17) · lines 540–551

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme assay and HPLC metabolite identification · source_derived_draft · unverified_draft

    ### coumarin-ugt-conjugation Bovine liver UGT preparation converted 7-hydroxycoumarin and UDP-glucuronic acid into its glucuronide. Condition category: normal nutrient_topic: Coumarin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A sugar-acid donor enables the conjugation step. organism: Bovine tissue_or_cell_type: Liver homogenate/crude UGT preparation experimental_model: Enzyme assay and HPLC metabolite identification limitations: Bovine preparation does not identify a dominant human UGT isoform. exposure: 7-Hydroxycoumarin plus UDP-glucuronic acid evidence_span: {"source_cache": "artifacts/coumarin-research/8877866.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8092618f6e2773ad94670c810fb44af7c2acedc0680674872af23af8bc55e26d", "start_char": 0, "end_char": 2114, "text_sha256": "8092618f6e2773ad94670c810fb44af7c2acedc0680674872af23af8bc55e26d"} [coumarin-p8877866] Analysis of the glucuronidation of 7-hydroxycoumarin by HPLC. (1996). https://pubmed.ncbi.nlm.nih.gov/8877866/ DOI: 10.1016/0731-7085(96)01801-8
    Complete structured claim and evidence

  14. Human UGT1A9 was a principal contributor to 10-gingerol 5-O-glucuronide formation in the enzyme comparison.

    10-Gingerol → 10-Gingerol 5-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    dose
    Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract
    duration
    Not specified in accessed abstract
    evidence_access
    Primary PubMed abstract.
    evidence_scope
    literature_reviewed; model-specific source-derived curation, not universally established human effects
    experimental_model
    Human liver microsomes and expressed human UGT enzymes
    limitations
    UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people.
    nutrient_topic
    Gingerols collection; each molecular form and experimental preparation remains explicit. · Gingerols
    organism
    Human liver microsomes and expressed human UGT enzymes
    plain_language
    Human UGT1A9 was a principal contributor to 10-gingerol 5-O-glucuronide formation in the enzyme comparison.
    primary_references
    Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351
    route
    In vitro incubation
    tissue
    Hepatic and recombinant enzyme preparations

    Gingerols: mechanisms, molecular forms and cross-actor connections (2026-09-20) · lines 338–347

    Original AI-assisted curation of thirteen primary research papers; study-specific PubMed/DOI links and limitations retained. Not publisher full text. · supports · Human liver microsomes and expressed human UGT enzymes · source_derived_draft · unverified_draft

    ## gingerols-10-ugt1a9 Human UGT1A9 was a principal contributor to 10-gingerol 5-O-glucuronide formation in the enzyme comparison. Model/species: Human liver microsomes and expressed human UGT enzymes Tissue: Hepatic and recombinant enzyme preparations Exposure: Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract Route: In vitro incubation Duration: Not specified in accessed abstract Limits: UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people. Primary reference: Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351 Access: Primary PubMed abstract.
    Complete structured claim and evidence

  15. Human UGT2B7 was a principal contributor to 10-gingerol 4-prime-O-glucuronide formation in the enzyme comparison.

    10-Gingerol → 10-Gingerol 4-prime-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    dose
    Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract
    duration
    Not specified in accessed abstract
    evidence_access
    Primary PubMed abstract.
    evidence_scope
    literature_reviewed; model-specific source-derived curation, not universally established human effects
    experimental_model
    Human liver microsomes and expressed human UGT enzymes
    limitations
    UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people.
    nutrient_topic
    Gingerols collection; each molecular form and experimental preparation remains explicit. · Gingerols
    organism
    Human liver microsomes and expressed human UGT enzymes
    plain_language
    Human UGT2B7 was a principal contributor to 10-gingerol 4-prime-O-glucuronide formation in the enzyme comparison.
    primary_references
    Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351
    route
    In vitro incubation
    tissue
    Hepatic and recombinant enzyme preparations

    Gingerols: mechanisms, molecular forms and cross-actor connections (2026-09-20) · lines 327–336

    Original AI-assisted curation of thirteen primary research papers; study-specific PubMed/DOI links and limitations retained. Not publisher full text. · supports · Human liver microsomes and expressed human UGT enzymes · source_derived_draft · unverified_draft

    ## gingerols-10-ugt2b7 Human UGT2B7 was a principal contributor to 10-gingerol 4-prime-O-glucuronide formation in the enzyme comparison. Model/species: Human liver microsomes and expressed human UGT enzymes Tissue: Hepatic and recombinant enzyme preparations Exposure: Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract Route: In vitro incubation Duration: Not specified in accessed abstract Limits: UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people. Primary reference: Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351 Access: Primary PubMed abstract.
    Complete structured claim and evidence

  16. UDP-glucuronic-acid-fortified human intestinal microsomes formed the phenolic 6-gingerol glucuronide.

    6-Gingerol → 6-Gingerol 4-prime-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    dose
    6-Gingerol with UDP-glucuronic acid; exact concentrations not in accessed abstract
    duration
    Not specified in accessed abstract
    evidence_access
    Primary PubMed abstract.
    evidence_scope
    literature_reviewed; model-specific source-derived curation, not universally established human effects
    experimental_model
    Human intestinal microsomes
    limitations
    Phenolic product formation in this preparation is not absolute oral bioavailability or a proven clinical interaction.
    nutrient_topic
    Gingerols collection; each molecular form and experimental preparation remains explicit. · Gingerols
    organism
    Human intestinal microsomes
    plain_language
    UDP-glucuronic-acid-fortified human intestinal microsomes formed the phenolic 6-gingerol glucuronide.
    primary_references
    Microsomal hydroxylation and glucuronidation of [6]-gingerol. (2006). https://pubmed.ncbi.nlm.nih.gov/17090120/ DOI: 10.1021/jf062235l
    route
    In vitro microsomal incubation
    tissue
    Intestinal microsomal preparation

    Gingerols: mechanisms, molecular forms and cross-actor connections (2026-09-20) · lines 272–281

    Original AI-assisted curation of thirteen primary research papers; study-specific PubMed/DOI links and limitations retained. Not publisher full text. · supports · Human intestinal microsomes · source_derived_draft · unverified_draft

    ## gingerols-6-intestinal-glucuronide UDP-glucuronic-acid-fortified human intestinal microsomes formed the phenolic 6-gingerol glucuronide. Model/species: Human intestinal microsomes Tissue: Intestinal microsomal preparation Exposure: 6-Gingerol with UDP-glucuronic acid; exact concentrations not in accessed abstract Route: In vitro microsomal incubation Duration: Not specified in accessed abstract Limits: Phenolic product formation in this preparation is not absolute oral bioavailability or a proven clinical interaction. Primary reference: Microsomal hydroxylation and glucuronidation of [6]-gingerol. (2006). https://pubmed.ncbi.nlm.nih.gov/17090120/ DOI: 10.1021/jf062235l Access: Primary PubMed abstract.
    Complete structured claim and evidence

  17. Human UGT1A9 was a principal contributor to 6-gingerol 5-O-glucuronide formation in the enzyme comparison.

    6-Gingerol → 6-Gingerol 5-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    dose
    Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract
    duration
    Not specified in accessed abstract
    evidence_access
    Primary PubMed abstract.
    evidence_scope
    literature_reviewed; model-specific source-derived curation, not universally established human effects
    experimental_model
    Human liver microsomes and expressed human UGT enzymes
    limitations
    UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people.
    nutrient_topic
    Gingerols collection; each molecular form and experimental preparation remains explicit. · Gingerols
    organism
    Human liver microsomes and expressed human UGT enzymes
    plain_language
    Human UGT1A9 was a principal contributor to 6-gingerol 5-O-glucuronide formation in the enzyme comparison.
    primary_references
    Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351
    route
    In vitro incubation
    tissue
    Hepatic and recombinant enzyme preparations

    Gingerols: mechanisms, molecular forms and cross-actor connections (2026-09-20) · lines 294–303

    Original AI-assisted curation of thirteen primary research papers; study-specific PubMed/DOI links and limitations retained. Not publisher full text. · supports · Human liver microsomes and expressed human UGT enzymes · source_derived_draft · unverified_draft

    ## gingerols-6-ugt1a9 Human UGT1A9 was a principal contributor to 6-gingerol 5-O-glucuronide formation in the enzyme comparison. Model/species: Human liver microsomes and expressed human UGT enzymes Tissue: Hepatic and recombinant enzyme preparations Exposure: Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract Route: In vitro incubation Duration: Not specified in accessed abstract Limits: UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people. Primary reference: Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351 Access: Primary PubMed abstract.
    Complete structured claim and evidence

  18. Human UGT2B7 was a principal contributor to 6-gingerol 4-prime-O-glucuronide formation in the enzyme comparison.

    6-Gingerol → 6-Gingerol 4-prime-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    dose
    Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract
    duration
    Not specified in accessed abstract
    evidence_access
    Primary PubMed abstract.
    evidence_scope
    literature_reviewed; model-specific source-derived curation, not universally established human effects
    experimental_model
    Human liver microsomes and expressed human UGT enzymes
    limitations
    UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people.
    nutrient_topic
    Gingerols collection; each molecular form and experimental preparation remains explicit. · Gingerols
    organism
    Human liver microsomes and expressed human UGT enzymes
    plain_language
    Human UGT2B7 was a principal contributor to 6-gingerol 4-prime-O-glucuronide formation in the enzyme comparison.
    primary_references
    Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351
    route
    In vitro incubation
    tissue
    Hepatic and recombinant enzyme preparations

    Gingerols: mechanisms, molecular forms and cross-actor connections (2026-09-20) · lines 283–292

    Original AI-assisted curation of thirteen primary research papers; study-specific PubMed/DOI links and limitations retained. Not publisher full text. · supports · Human liver microsomes and expressed human UGT enzymes · source_derived_draft · unverified_draft

    ## gingerols-6-ugt2b7 Human UGT2B7 was a principal contributor to 6-gingerol 4-prime-O-glucuronide formation in the enzyme comparison. Model/species: Human liver microsomes and expressed human UGT enzymes Tissue: Hepatic and recombinant enzyme preparations Exposure: Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract Route: In vitro incubation Duration: Not specified in accessed abstract Limits: UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people. Primary reference: Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351 Access: Primary PubMed abstract.
    Complete structured claim and evidence

  19. Human UGT1A9 was a principal contributor to 8-gingerol 5-O-glucuronide formation in the enzyme comparison.

    8-Gingerol → 8-Gingerol 5-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    dose
    Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract
    duration
    Not specified in accessed abstract
    evidence_access
    Primary PubMed abstract.
    evidence_scope
    literature_reviewed; model-specific source-derived curation, not universally established human effects
    experimental_model
    Human liver microsomes and expressed human UGT enzymes
    limitations
    UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people.
    nutrient_topic
    Gingerols collection; each molecular form and experimental preparation remains explicit. · Gingerols
    organism
    Human liver microsomes and expressed human UGT enzymes
    plain_language
    Human UGT1A9 was a principal contributor to 8-gingerol 5-O-glucuronide formation in the enzyme comparison.
    primary_references
    Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351
    route
    In vitro incubation
    tissue
    Hepatic and recombinant enzyme preparations

    Gingerols: mechanisms, molecular forms and cross-actor connections (2026-09-20) · lines 316–325

    Original AI-assisted curation of thirteen primary research papers; study-specific PubMed/DOI links and limitations retained. Not publisher full text. · supports · Human liver microsomes and expressed human UGT enzymes · source_derived_draft · unverified_draft

    ## gingerols-8-ugt1a9 Human UGT1A9 was a principal contributor to 8-gingerol 5-O-glucuronide formation in the enzyme comparison. Model/species: Human liver microsomes and expressed human UGT enzymes Tissue: Hepatic and recombinant enzyme preparations Exposure: Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract Route: In vitro incubation Duration: Not specified in accessed abstract Limits: UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people. Primary reference: Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351 Access: Primary PubMed abstract.
    Complete structured claim and evidence

  20. Human UGT2B7 was a principal contributor to 8-gingerol 4-prime-O-glucuronide formation in the enzyme comparison.

    8-Gingerol → 8-Gingerol 4-prime-O-glucuronide source_derived_draftungraded
    Experimental context and source evidence
    dose
    Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract
    duration
    Not specified in accessed abstract
    evidence_access
    Primary PubMed abstract.
    evidence_scope
    literature_reviewed; model-specific source-derived curation, not universally established human effects
    experimental_model
    Human liver microsomes and expressed human UGT enzymes
    limitations
    UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people.
    nutrient_topic
    Gingerols collection; each molecular form and experimental preparation remains explicit. · Gingerols
    organism
    Human liver microsomes and expressed human UGT enzymes
    plain_language
    Human UGT2B7 was a principal contributor to 8-gingerol 4-prime-O-glucuronide formation in the enzyme comparison.
    primary_references
    Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351
    route
    In vitro incubation
    tissue
    Hepatic and recombinant enzyme preparations

    Gingerols: mechanisms, molecular forms and cross-actor connections (2026-09-20) · lines 305–314

    Original AI-assisted curation of thirteen primary research papers; study-specific PubMed/DOI links and limitations retained. Not publisher full text. · supports · Human liver microsomes and expressed human UGT enzymes · source_derived_draft · unverified_draft

    ## gingerols-8-ugt2b7 Human UGT2B7 was a principal contributor to 8-gingerol 4-prime-O-glucuronide formation in the enzyme comparison. Model/species: Human liver microsomes and expressed human UGT enzymes Tissue: Hepatic and recombinant enzyme preparations Exposure: Individual 6-, 8- or 10-gingerol with UDP-glucuronic acid; exact concentration series not in accessed abstract Route: In vitro incubation Duration: Not specified in accessed abstract Limits: UGT2B7 favors but is not exclusive to 4-prime conjugation; UGT1A9 mainly forms 5-O conjugates. Shared UGT substrates do not prove competition in people. Primary reference: Regioselective glucuronidation of gingerols by human liver microsomes and expressed UDP-glucuronosyltransferase enzymes: reaction kinetics and activity correlation analyses for UGT1A9 and UGT2B7. (2015). https://pubmed.ncbi.nlm.nih.gov/25496264/ DOI: 10.1111/jphp.12351 Access: Primary PubMed abstract.
    Complete structured claim and evidence

In the sources

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

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