Component
Human succinyl-CoA:3-ketoacid CoA transferase / OXCT1
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 it acts on
G219E and G324E constructs had no detectable SCOT activity; patients had episodic ketoacidosis.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary abstract
- experimental_model
- Three SCOT-deficient patients and mutant expression in fibroblasts.
- limitations
- Rare genetic disease, not nutritional ketosis in healthy adults.
- nutrient_topic
- Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
- plain_language
- Ketones can accumulate when utilization machinery fails.
- primary_references
- Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT gene, tertiary structural modeling of the human SCOT monomer, and characterization of three pathogenic mutations. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10964512/ · DOI 10.1006/geno.2000.6282
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 152–158
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Three SCOT-deficient patients and mutant expression in fibroblasts. · source_derived_draft · unverified_draft
## fast-scot-defect Ketones can accumulate when utilization machinery fails. G219E and G324E constructs had no detectable SCOT activity; patients had episodic ketoacidosis. Model: Three SCOT-deficient patients and mutant expression in fibroblasts. Limitations: Rare genetic disease, not nutritional ketosis in healthy adults. Evidence access: Primary abstract Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT gene, tertiary structural modeling of the human SCOT monomer, and characterization of three pathogenic mutations. · 2000 · https://pubmed.ncbi.nlm.nih.gov/10964512/ · DOI 10.1006/geno.2000.6282
Complete structured claim and evidence
Where it participates (unsigned role)
OXCT1 transfers CoA from succinyl-CoA to acetoacetate, yielding acetoacetyl-CoA and succinate.
Experimental context and source evidence
- evidence_access
- Primary abstract and indexed full-text introduction, PMC3825524
- experimental_model
- Human SCOT structure; described ketolysis reaction.
- limitations
- Production of ketones and ability to use them are different capacities.
- nutrient_topic
- Fasting physiological-state collection; human protocols, cellular deprivation and refeeding are distinguished. · Fasting / abstention from energy intake
- plain_language
- Using ketones requires a separate activation step.
- primary_references
- A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23420214/ · DOI 10.1007/s10545-013-9589-z
Fasting: fuel switching, nutrient sensing, ketone signaling, nutrient dependencies and refeeding (2026-09-18) · lines 144–150
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human SCOT structure; described ketolysis reaction. · source_derived_draft · unverified_draft
## fast-scot Using ketones requires a separate activation step. OXCT1 transfers CoA from succinyl-CoA to acetoacetate, yielding acetoacetyl-CoA and succinate. Model: Human SCOT structure; described ketolysis reaction. Limitations: Production of ketones and ability to use them are different capacities. Evidence access: Primary abstract and indexed full-text introduction, PMC3825524 A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23420214/ · DOI 10.1007/s10545-013-9589-z
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.