Component

Human UDP-glucuronosyltransferase 2B7 / UGT2B7

Human UDP-glucuronosyltransferase 2B7 / UGT2B7. Species, exposure and limitations are retained in each linked claim.

8 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. UGT2B7 supported curcumin glucuronidation in the experimental system.

    Human UDP-glucuronosyltransferase 2B7 / UGT2B7 → Curcumin source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/curcumin-research/38522299.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "84f7b5a7112090e4cc09dfd8b0bfce03908e6dd800773861d42815d71caf261c", "start_char": 0, "end_char": 1005, "text_sha256": "84f7b5a7112090e4cc09dfd8b0bfce03908e6dd800773861d42815d71caf261c"}
    experimental_model
    Glucuronidation assays with human liver microsomes and UGT2B7
    exposure
    Curcumin compared with tetrahydrocurcumin; pH-dependent structural analysis
    limitations
    Kinetic and structural comparisons do not establish comparative clinical efficacy; docking hypotheses are not imported as proven steps.
    nutrient_topic
    Curcumin research collection; topical membership is not evidence of a direct dietary effect. · Curcumin
    organism
    Human tissue and enzyme systems
    plain_language
    A named enzyme contributes to curcumin conjugation.
    primary_references
    [curcumin-p38522299] Glucuronidation dynamics of curcumin and tetrahydrocurcumin for differential structures and chemical reactivities in human liver microsome and uridine diphosphate glucuronosyltransferase 2B7. (2024). https://pubmed.ncbi.nlm.nih.gov/38522299/ DOI: 10.1016/j.foodchem.2024.138929
    tissue_or_cell_type
    Microsomes and recombinant UGT2B7

    Curcumin: metabolism, signaling and nutrient connections (2026-09-17) · lines 177–188

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Glucuronidation assays with human liver microsomes and UGT2B7 · source_derived_draft · unverified_draft

    ### curcumin-ugt2b7-cur UGT2B7 supported curcumin glucuronidation in the experimental system. Condition category: normal nutrient_topic: Curcumin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A named enzyme contributes to curcumin conjugation. organism: Human tissue and enzyme systems tissue_or_cell_type: Microsomes and recombinant UGT2B7 experimental_model: Glucuronidation assays with human liver microsomes and UGT2B7 limitations: Kinetic and structural comparisons do not establish comparative clinical efficacy; docking hypotheses are not imported as proven steps. exposure: Curcumin compared with tetrahydrocurcumin; pH-dependent structural analysis evidence_span: {"source_cache": "artifacts/curcumin-research/38522299.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "84f7b5a7112090e4cc09dfd8b0bfce03908e6dd800773861d42815d71caf261c", "start_char": 0, "end_char": 1005, "text_sha256": "84f7b5a7112090e4cc09dfd8b0bfce03908e6dd800773861d42815d71caf261c"} [curcumin-p38522299] Glucuronidation dynamics of curcumin and tetrahydrocurcumin for differential structures and chemical reactivities in human liver microsome and uridine diphosphate glucuronosyltransferase 2B7. (2024). https://pubmed.ncbi.nlm.nih.gov/38522299/ DOI: 10.1016/j.foodchem.2024.138929
    Complete structured claim and evidence

  2. Tetrahydrocurcumin showed lower glucuronidation activity than curcumin under the tested UGT2B7 conditions.

    Human UDP-glucuronosyltransferase 2B7 / UGT2B7 → Tetrahydrocurcumin source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/curcumin-research/38522299.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "84f7b5a7112090e4cc09dfd8b0bfce03908e6dd800773861d42815d71caf261c", "start_char": 0, "end_char": 1005, "text_sha256": "84f7b5a7112090e4cc09dfd8b0bfce03908e6dd800773861d42815d71caf261c"}
    experimental_model
    Glucuronidation assays with human liver microsomes and UGT2B7
    exposure
    Curcumin compared with tetrahydrocurcumin; pH-dependent structural analysis
    limitations
    Kinetic and structural comparisons do not establish comparative clinical efficacy; docking hypotheses are not imported as proven steps.
    nutrient_topic
    Curcumin research collection; topical membership is not evidence of a direct dietary effect. · Curcumin
    organism
    Human tissue and enzyme systems
    plain_language
    The reduced metabolite is processed differently.
    primary_references
    [curcumin-p38522299] Glucuronidation dynamics of curcumin and tetrahydrocurcumin for differential structures and chemical reactivities in human liver microsome and uridine diphosphate glucuronosyltransferase 2B7. (2024). https://pubmed.ncbi.nlm.nih.gov/38522299/ DOI: 10.1016/j.foodchem.2024.138929
    tissue_or_cell_type
    Microsomes and recombinant UGT2B7

    Curcumin: metabolism, signaling and nutrient connections (2026-09-17) · lines 190–201

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Glucuronidation assays with human liver microsomes and UGT2B7 · source_derived_draft · unverified_draft

    ### curcumin-ugt2b7-thc Tetrahydrocurcumin showed lower glucuronidation activity than curcumin under the tested UGT2B7 conditions. Condition category: normal nutrient_topic: Curcumin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The reduced metabolite is processed differently. organism: Human tissue and enzyme systems tissue_or_cell_type: Microsomes and recombinant UGT2B7 experimental_model: Glucuronidation assays with human liver microsomes and UGT2B7 limitations: Kinetic and structural comparisons do not establish comparative clinical efficacy; docking hypotheses are not imported as proven steps. exposure: Curcumin compared with tetrahydrocurcumin; pH-dependent structural analysis evidence_span: {"source_cache": "artifacts/curcumin-research/38522299.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "84f7b5a7112090e4cc09dfd8b0bfce03908e6dd800773861d42815d71caf261c", "start_char": 0, "end_char": 1005, "text_sha256": "84f7b5a7112090e4cc09dfd8b0bfce03908e6dd800773861d42815d71caf261c"} [curcumin-p38522299] Glucuronidation dynamics of curcumin and tetrahydrocurcumin for differential structures and chemical reactivities in human liver microsome and uridine diphosphate glucuronosyltransferase 2B7. (2024). https://pubmed.ncbi.nlm.nih.gov/38522299/ DOI: 10.1016/j.foodchem.2024.138929
    Complete structured claim and evidence

  3. 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

What acts on it

  1. At 250 micrograms/mL, mangiferin reduced UGT2B7 activity by about 55 percent.

    Mangiferin → Human UDP-glucuronosyltransferase 2B7 / UGT2B7 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 848–859

    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-ugt2b7-activity At 250 micrograms/mL, mangiferin reduced UGT2B7 activity by about 55 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. Diclofenac inhibited steviol glucuronidation in human liver microsomes, with reported Ki 4.2 micromolar.

    Diclofenac → Human microsomal steviol glucuronidation source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    In vitro human liver microsomes.
    limitations
    Clinical relevance at ordinary sweetener exposure was not established; steviol is the possible interaction victim.
    nutrient_topic
    Stevia collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · Stevia
    plain_language
    A drug can interfere with the clearance step for a plant-derived metabolite.
    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 66–72

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · In vitro human liver microsomes. · source_derived_draft · unverified_draft

    ## stevia-diclofenac-conjugation A drug can interfere with the clearance step for a plant-derived metabolite. Diclofenac inhibited steviol glucuronidation in human liver microsomes, with reported Ki 4.2 micromolar. Model: In vitro human liver microsomes. Limitations: Clinical relevance at ordinary sweetener exposure was not established; steviol is the possible interaction victim. 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

  2. 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

  3. 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

  4. 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

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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