Component
Human mitochondrial D-beta-hydroxybutyrate dehydrogenase / BDH1
Context-specific entity; species, compartment and exposure are stated on each 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.
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-heart mitochondrial BDH1 was described as specifically requiring phosphatidylcholine for enzymic activity.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Primary human-heart enzyme cloning and characterization.
- limitations
- Does not establish that supplemental choline increases ketone use.
- nutrient_topic
- Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
- plain_language
- A membrane lipid linked to choline supports a ketone enzyme.
- primary_references
- Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart. · 1992 · https://pubmed.ncbi.nlm.nih.gov/1639787/
Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 136–142
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Primary human-heart enzyme cloning and characterization. · source_derived_draft · unverified_draft
## fast-bdh-choline A membrane lipid linked to choline supports a ketone enzyme. Human-heart mitochondrial BDH1 was described as specifically requiring phosphatidylcholine for enzymic activity. Model: Primary human-heart enzyme cloning and characterization. Limitations: Does not establish that supplemental choline increases ketone use. Evidence access: Primary abstract Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart. · 1992 · https://pubmed.ncbi.nlm.nih.gov/1639787/
Complete structured claim and evidence
Where it participates (unsigned role)
BDH1 interconverts D-beta-hydroxybutyrate and acetoacetate using the NAD+/NADH redox pair.
Experimental context and source evidence
- evidence_access
- Reactome curated reaction and its primary-study attribution
- experimental_model
- Curated human mitochondrial reaction R-HSA-73920; cites human-heart BDH1 work.
- limitations
- Reversible reaction; redox state and compartment determine net direction.
- nutrient_topic
- Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
- plain_language
- Ketone interconversion connects to niacin-derived redox chemistry.
- primary_references
- BDH1: D-beta-hydroxybutyrate + NAD+ ⇌ acetoacetate + NADH + H+ · 2003 · https://reactome.org/content/detail/R-HSA-73920
Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 128–134
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Curated human mitochondrial reaction R-HSA-73920; cites human-heart BDH1 work. · source_derived_draft · unverified_draft
## fast-bdh-reaction Ketone interconversion connects to niacin-derived redox chemistry. BDH1 interconverts D-beta-hydroxybutyrate and acetoacetate using the NAD+/NADH redox pair. Model: Curated human mitochondrial reaction R-HSA-73920; cites human-heart BDH1 work. Limitations: Reversible reaction; redox state and compartment determine net direction. Evidence access: Reactome curated reaction and its primary-study attribution BDH1: D-beta-hydroxybutyrate + NAD+ ⇌ acetoacetate + NADH + H+ · 2003 · https://reactome.org/content/detail/R-HSA-73920
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.