Component

Human carnitine acetyltransferase / CRAT

Context-specific entity; species, compartment and exposure are stated on each claim.

4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What it acts on

  1. Silencing CRAT in primary human myotubes reduced acetylcarnitine export by 47%.

    Human carnitine acetyltransferase / CRAT → Human primary myotube acetylcarnitine export source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text Figure 6 and methods
    experimental_model
    Human myotubes; adenoviral silencing, approximately 60% lower enzyme activity.
    limitations
    Cell culture, not human supplementation.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    An independent enzyme controls acetyl-group export from muscle cells.
    primary_references
    Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 170–176

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human myotubes; adenoviral silencing, approximately 60% lower enzyme activity. · source_derived_draft · unverified_draft

    ## l-carnitine-crat-knockdown-export An independent enzyme controls acetyl-group export from muscle cells. Silencing CRAT in primary human myotubes reduced acetylcarnitine export by 47%. Model: Human myotubes; adenoviral silencing, approximately 60% lower enzyme activity. Limitations: Cell culture, not human supplementation. Evidence access: Primary full-text Figure 6 and methods Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005
    Complete structured claim and evidence

  2. Silencing CRAT in human myotubes reduced glucose uptake by 13% while increasing oleate oxidation.

    Human carnitine acetyltransferase / CRAT → Human primary myotube glucose uptake source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text Figure 6
    experimental_model
    Primary human myotube loss-of-function experiment.
    limitations
    No universal reciprocal rule for all tissues.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    More fat oxidation did not mean better glucose handling in this experiment.
    primary_references
    Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 178–184

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Primary human myotube loss-of-function experiment. · source_derived_draft · unverified_draft

    ## l-carnitine-crat-knockdown-glucose More fat oxidation did not mean better glucose handling in this experiment. Silencing CRAT in human myotubes reduced glucose uptake by 13% while increasing oleate oxidation. Model: Primary human myotube loss-of-function experiment. Limitations: No universal reciprocal rule for all tissues. Evidence access: Primary full-text Figure 6 Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005
    Complete structured claim and evidence

  3. Deleting CRAT did not diminish acetyl-CoA labeling from supplied acetylcarnitine in U87MG cells.

    Human carnitine acetyltransferase / CRAT → Human U87MG acetyl-CoA labeling from acetylcarnitine source_derived_draftungraded
    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

  4. Purified recombinant human CRAT transferred short-chain acyl groups including acetyl from acyl-CoA substrates to carnitine in enzyme assays.

    Human carnitine acetyltransferase / CRAT → Acetyl-L-carnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text Table 1 and recombinant enzyme methods
    experimental_model
    Human CRAT expressed in E. coli; steady-state kinetic substrate panel.
    limitations
    Purified-enzyme capacity does not identify the dominant flux in every compartment.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The human enzyme directly connects carnitine and the CoA pool.
    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 498–504

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human CRAT expressed in E. coli; steady-state kinetic substrate panel. · source_derived_draft · unverified_draft

    ## l-carnitine-human-crat-reaction The human enzyme directly connects carnitine and the CoA pool. Purified recombinant human CRAT transferred short-chain acyl groups including acetyl from acyl-CoA substrates to carnitine in enzyme assays. Model: Human CRAT expressed in E. coli; steady-state kinetic substrate panel. Limitations: Purified-enzyme capacity does not identify the dominant flux in every compartment. Evidence access: Primary full-text Table 1 and recombinant enzyme methods 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

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards