Component
24-Hydroxyvitamin D2
D2 side-chain hydroxylation product distinguished from its 25-hydroxylated precursor route.
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
Human CYP27A1 hydroxylated ergocalciferol at C24 in the reported D2 substrate analysis.
Experimental context and source evidence
- cross_nutrient
- false
- evidence_location
- Primary abstract, substrate product positions and kinetic comparison.
- experimental_model
- Recombinant human CYP27A1 product identification
- exposure
- D2 incubation; concentration/time not reported in retrieved abstract.
- limitations
- D2 C24/C27 hydroxylation must not be mislabeled as C25 activation or assumed to be the main route in vivo.
- nutrient
- Vitamin D2 and D3 · Vitamin D2 and D3
- nutrient_topic
- Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin D2 and D3
- organism
- Homo sapiens protein
- plain_language
- CYP27A1 modifies D2 at carbon 24.
- primary_references
- [shinkyo2004] Metabolism of vitamin D by human microsomal CYP2R1. (2004). https://pubmed.ncbi.nlm.nih.gov/15465040/ DOI: 10.1016/j.bbrc.2004.09.073
- tissue_or_cell_type
- mitochondrial enzyme preparation
Vitamin D2 and D3: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 332–345
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human CYP27A1 product identification · source_derived_draft · unverified_draft
### vd-act-cyp27a1-d2-c24 Human CYP27A1 hydroxylated ergocalciferol at C24 in the reported D2 substrate analysis. Condition category: normal nutrient_topic: Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. plain_language: CYP27A1 modifies D2 at carbon 24. organism: Homo sapiens protein tissue_or_cell_type: mitochondrial enzyme preparation experimental_model: Recombinant human CYP27A1 product identification limitations: D2 C24/C27 hydroxylation must not be mislabeled as C25 activation or assumed to be the main route in vivo. exposure: D2 incubation; concentration/time not reported in retrieved abstract. cross_nutrient: false evidence_location: Primary abstract, substrate product positions and kinetic comparison. nutrient: Vitamin D2 and D3 [shinkyo2004] Metabolism of vitamin D by human microsomal CYP2R1. (2004). https://pubmed.ncbi.nlm.nih.gov/15465040/ DOI: 10.1016/j.bbrc.2004.09.073
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.