Component

Human UDP-glucuronosyltransferase 1A9 / UGT1A9

Human UDP-glucuronosyltransferase 1A9 / UGT1A9. Species, exposure and limitations are retained in each linked claim.

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

Read recorded mechanisms Open recursive mind map

How nutrients influence it

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

How nutrients reach it in more than one step

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

Tracing routes…

What it does

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

Recorded relationships

What it acts on

  1. 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

  2. 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

  3. 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

  4. 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

  5. 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

  6. 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

What acts on it

  1. Norathyriol competitively inhibited UGT1A9; IC50 12.3 and Ki 2.8 micromolar.

    Norathyriol → Human UDP-glucuronosyltransferase 1A9 / UGT1A9 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/mangiferin-research/28621744.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e2741f9036a84104809f4d9813afeb1603b3e93e1d247ea0e4b5ff31be0e1ae5", "start_char": 0, "end_char": 1562, "text_sha256": "e2741f9036a84104809f4d9813afeb1603b3e93e1d247ea0e4b5ff31be0e1ae5"}
    experimental_model
    Recombinant UGT inhibition kinetics
    exposure
    Micromolar norathyriol; initial comparison at 100 micromolar
    limitations
    Probe-dependent biochemical inhibition; no established human interaction threshold. Docking is not additional proof of binding in vivo.
    nutrient_topic
    Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
    organism
    Recombinant enzyme assay
    plain_language
    The aglycone has its own conjugation-enzyme interaction profile.
    primary_references
    [mangiferin-p28621744] In Vitro Comparative Study of the Inhibitory Effects of Mangiferin and Its Aglycone Norathyriol towards UDP-Glucuronosyl Transferase (UGT) Isoforms. (2017). https://pubmed.ncbi.nlm.nih.gov/28621744/ DOI: 10.3390/molecules22061008
    tissue_or_cell_type
    4-methylumbelliferone glucuronidation

    Mangiferin: metabolism, signaling and nutrient connections (2026-09-17) · lines 900–911

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant UGT inhibition kinetics · source_derived_draft · unverified_draft

    ### mangiferin-norathyriol-ugt1a9 Norathyriol competitively inhibited UGT1A9; IC50 12.3 and Ki 2.8 micromolar. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The aglycone has its own conjugation-enzyme interaction profile. organism: Recombinant enzyme assay tissue_or_cell_type: 4-methylumbelliferone glucuronidation experimental_model: Recombinant UGT inhibition kinetics limitations: Probe-dependent biochemical inhibition; no established human interaction threshold. Docking is not additional proof of binding in vivo. exposure: Micromolar norathyriol; initial comparison at 100 micromolar evidence_span: {"source_cache": "artifacts/mangiferin-research/28621744.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e2741f9036a84104809f4d9813afeb1603b3e93e1d247ea0e4b5ff31be0e1ae5", "start_char": 0, "end_char": 1562, "text_sha256": "e2741f9036a84104809f4d9813afeb1603b3e93e1d247ea0e4b5ff31be0e1ae5"} [mangiferin-p28621744] In Vitro Comparative Study of the Inhibitory Effects of Mangiferin and Its Aglycone Norathyriol towards UDP-Glucuronosyl Transferase (UGT) Isoforms. (2017). https://pubmed.ncbi.nlm.nih.gov/28621744/ DOI: 10.3390/molecules22061008
    Complete structured claim and evidence

  2. At 250 micrograms/mL, mangiferin reduced UGT1A9 activity by about 35 percent.

    Mangiferin → Human UDP-glucuronosyltransferase 1A9 / UGT1A9 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/mangiferin-research/22815239.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0", "start_char": 0, "end_char": 1728, "text_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0"}
    experimental_model
    Primary human hepatocyte exposure
    exposure
    Mangiferin 50-250 micrograms/mL for 48 hours
    limitations
    High in vitro concentrations; decreased enzyme activity is not proof of human drug-level changes. Extract and isolated mangiferin are distinct.
    nutrient_topic
    Mangiferin research collection; topical membership is not evidence of a direct dietary effect. · Mangiferin
    organism
    Homo sapiens
    plain_language
    A conjugation pathway also responded in vitro.
    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 861–872

    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-ugt1a9-activity At 250 micrograms/mL, mangiferin reduced UGT1A9 activity by about 35 percent. Condition category: normal nutrient_topic: Mangiferin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A conjugation pathway also responded in vitro. organism: Homo sapiens tissue_or_cell_type: Cultured hepatocytes experimental_model: Primary human hepatocyte exposure limitations: High in vitro concentrations; decreased enzyme activity is not proof of human drug-level changes. Extract and isolated mangiferin are distinct. exposure: Mangiferin 50-250 micrograms/mL for 48 hours evidence_span: {"source_cache": "artifacts/mangiferin-research/22815239.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0", "start_char": 0, "end_char": 1728, "text_sha256": "e85ebd0af89f030dbeda45ed922e93a8a616c51f5ce1b64badc44d90791716c0"} [mangiferin-p22815239] Mangifera indica L. extract and mangiferin modulate cytochrome P450 and UDP-glucuronosyltransferase enzymes in primary cultures of human hepatocytes. (2013). https://pubmed.ncbi.nlm.nih.gov/22815239/ DOI: 10.1002/ptr.4782
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. 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

  2. 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

  3. 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

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

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

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