Component

Human UDP-glucuronosyltransferase 1A3 / UGT1A3

Human UDP-glucuronosyltransferase 1A3 / UGT1A3. Species, exposure and limitations are retained in each linked claim.

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

How nutrients influence it

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

How nutrients reach it in more than one step

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

Tracing routes…

What it does

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

Recorded relationships

What it acts on

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

    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

What acts on it

  1. Norathyriol competitively inhibited UGT1A3; IC50 8.2 and Ki 1.6 micromolar.

    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 874–885

    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-ugt1a3 Norathyriol competitively inhibited UGT1A3; IC50 8.2 and Ki 1.6 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

In the sources

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

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

    Evidence, AI assistance and curation standards