Component
13′-Hydroxy-alpha-tocopherol
Initial terminal side-chain hydroxylation product of alpha-tocopherol; not alpha-CEHC.
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.
What acts on it
Recombinant human CYP4F2 catalyzed terminal side-chain hydroxylation of alpha-tocopherol to its 13′-hydroxy product.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- Recombinant human P450 enzyme comparison
- exposure
- alpha-Tocopherol substrate with NADPH; quantitative incubation details not assigned here.
- limitations
- Initial oxidation only; other enzymes perform subsequent side-chain shortening.
- nutrient_topic
- Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
- organism
- Human protein in recombinant microsomes
- plain_language
- CYP4F2 begins breakdown of this tocopherol form.
- primary_references
- [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
- tissue_or_cell_type
- Microsomal enzyme preparation
Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 402–413
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human P450 enzyme comparison · source_derived_draft · unverified_draft
### ve-transport-cyp4f2-alpha-hydroxylation Recombinant human CYP4F2 catalyzed terminal side-chain hydroxylation of alpha-tocopherol to its 13′-hydroxy product. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: CYP4F2 begins breakdown of this tocopherol form. organism: Human protein in recombinant microsomes tissue_or_cell_type: Microsomal enzyme preparation experimental_model: Recombinant human P450 enzyme comparison limitations: Initial oxidation only; other enzymes perform subsequent side-chain shortening. exposure: alpha-Tocopherol substrate with NADPH; quantitative incubation details not assigned here. cross_nutrient: false [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
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.