Component
Human carnitine octanoyltransferase / CROT
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
Deleting CROT reduced labeling of acetyl-CoA and palmitate from exogenous acetylcarnitine; CROT cDNA rescue restored acetyl-CoA labeling.
Experimental context and source evidence
- evidence_access
- Primary full-text Figure 5 and enzyme assays
- experimental_model
- Human U87MG cells, CROT knockout and rescue; 1 mM tracer under glucose limitation.
- limitations
- Compartment and substrate supply may explain why this enzyme dominates in these cells.
- nutrient_topic
- L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
- plain_language
- Another carnitine enzyme provided this carbon route.
- primary_references
- Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848
L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 218–224
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human U87MG cells, CROT knockout and rescue; 1 mM tracer under glucose limitation. · source_derived_draft · unverified_draft
## l-carnitine-crot-knockout Another carnitine enzyme provided this carbon route. Deleting CROT reduced labeling of acetyl-CoA and palmitate from exogenous acetylcarnitine; CROT cDNA rescue restored acetyl-CoA labeling. Model: Human U87MG cells, CROT knockout and rescue; 1 mM tracer under glucose limitation. Limitations: Compartment and substrate supply may explain why this enzyme dominates in these cells. Evidence access: Primary full-text Figure 5 and enzyme assays Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848
Complete structured claim and evidence
Where it participates (unsigned role)
Deleting CRAT did not diminish acetyl-CoA labeling from supplied acetylcarnitine in U87MG cells.
Experimental context and source evidence
- evidence_access
- Primary full-text Figure 4
- experimental_model
- Human U87MG knockout and tracer experiment.
- limitations
- Incoming acetylcarnitine utilization differs from mitochondrial production; not a conflict with muscle export.
- nutrient_topic
- L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
- plain_language
- The enzyme needed to make acetylcarnitine need not be the one that uses it.
- primary_references
- Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848
L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 226–232
AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human U87MG knockout and tracer experiment. · source_derived_draft · unverified_draft
## l-carnitine-crat-null-assimilation The enzyme needed to make acetylcarnitine need not be the one that uses it. Deleting CRAT did not diminish acetyl-CoA labeling from supplied acetylcarnitine in U87MG cells. Model: Human U87MG knockout and tracer experiment. Limitations: Incoming acetylcarnitine utilization differs from mitochondrial production; not a conflict with muscle export. Evidence access: Primary full-text Figure 4 Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848
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.