Component
Human sulfotransferase 2A1 / SULT2A1
Study-scoped entity; inspect species, exposure, model and limitations on each claim.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
Where it participates (unsigned role)
The 2016 SULT1A1 allostery study explicitly reported that EGCG was not a SULT1A1 substrate but was sulfonated by SULT2A1.
Experimental context and source evidence
- experimental_model
- Equilibrium binding and pre-steady-state human SULT enzyme experiments.
- limitations
- This differs from the later SULT1A1 assignment; assay and product-identification differences require comparison.
- nutrient_topic
- EGCG collection; comparator and shared-pathway records retain their actual intervention. · Epigallocatechin-3-gallate (EGCG)
- plain_language
- An earlier enzyme study gives a different substrate assignment.
- primary_references
- Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27356022/ · DOI 10.1021/acs.biochem.6b00401
EGCG: receptor signaling, metabolism, nutrient interactions and discovery questions (2026-09-18) · lines 300–306
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Equilibrium binding and pre-steady-state human SULT enzyme experiments. · source_derived_draft · unverified_draft
## egcg-sult-not-substrate An earlier enzyme study gives a different substrate assignment. The 2016 SULT1A1 allostery study explicitly reported that EGCG was not a SULT1A1 substrate but was sulfonated by SULT2A1. Model: Equilibrium binding and pre-steady-state human SULT enzyme experiments. Limitations: This differs from the later SULT1A1 assignment; assay and product-identification differences require comparison. Evidence access: primary abstract. Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27356022/ · DOI 10.1021/acs.biochem.6b00401
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.