Component

Palmitoyl-CoA

Acyl donor represented as an independent event participant.

5 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

Where it participates (unsigned role)

  1. PLP-dependent human SPT condenses serine and palmitoyl-CoA into 3-ketosphinganine; the product-bound structure locates its headgroup and acyl chain.

    Human SPTLC1-SPTLC2-SPTSSA complex → 3-Ketosphinganine source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    B6-dependent use of the amino acid serine and a fatty-acyl-CoA substrate.
    experimental_model
    Recombinant human SPT complexes; cryo-EM and cell/microsome activity assays
    exposure
    Product-bound cryo-EM and functional enzyme assays.
    limitations
    Does not show that B6 supplementation repairs myelin.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Homo sapiens
    plain_language
    B6 supports entry into sphingolipid synthesis.
    primary_references
    [wang-2021-spt] Structural insights into the regulation of human serine palmitoyltransferase complexes (2021). https://pmc.ncbi.nlm.nih.gov/articles/PMC9812531/ DOI: 10.1038/s41594-020-00551-9
    tissue_or_cell_type
    Purified recombinant protein; no intact tissue

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1120–1131

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human SPT complexes; cryo-EM and cell/microsome activity assays · source_derived_draft · unverified_draft

    ### b6-neuro-spt-sphingolipid-entry PLP-dependent human SPT condenses serine and palmitoyl-CoA into 3-ketosphinganine; the product-bound structure locates its headgroup and acyl chain. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: B6 supports entry into sphingolipid synthesis. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Recombinant human SPT complexes; cryo-EM and cell/microsome activity assays limitations: Does not show that B6 supplementation repairs myelin. exposure: Product-bound cryo-EM and functional enzyme assays. cross_nutrient: B6-dependent use of the amino acid serine and a fatty-acyl-CoA substrate. [wang-2021-spt] Structural insights into the regulation of human serine palmitoyltransferase complexes (2021). https://pmc.ncbi.nlm.nih.gov/articles/PMC9812531/ DOI: 10.1038/s41594-020-00551-9
    Complete structured claim and evidence

  2. Human CPT1B expressed in yeast catalyzed transfer from palmitoyl-CoA onto carnitine, forming palmitoylcarnitine and releasing CoA.

    Human carnitine palmitoyltransferase 1B / CPT1B → L-Carnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and reviewed UniProt catalytic-reaction record
    experimental_model
    Human heart/muscle isoform in Pichia mitochondria; canonical reaction also recorded in UniProt Q92523/Rhea 12661.
    limitations
    This isoform assay does not measure whole-body fat loss.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The outer-membrane enzyme loads a fatty-acid group onto carnitine.
    primary_references
    Functional studies of yeast-expressed human heart muscle carnitine palmitoyltransferase I. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9344464/ · DOI 10.1006/abbi.1997.0314

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 90–96

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human heart/muscle isoform in Pichia mitochondria; canonical reaction also recorded in UniProt Q92523/Rhea 12661. · source_derived_draft · unverified_draft

    ## l-carnitine-cpt1-transfer The outer-membrane enzyme loads a fatty-acid group onto carnitine. Human CPT1B expressed in yeast catalyzed transfer from palmitoyl-CoA onto carnitine, forming palmitoylcarnitine and releasing CoA. Model: Human heart/muscle isoform in Pichia mitochondria; canonical reaction also recorded in UniProt Q92523/Rhea 12661. Limitations: This isoform assay does not measure whole-body fat loss. Evidence access: Primary abstract and reviewed UniProt catalytic-reaction record Functional studies of yeast-expressed human heart muscle carnitine palmitoyltransferase I. · 1997 · https://pubmed.ncbi.nlm.nih.gov/9344464/ · DOI 10.1006/abbi.1997.0314
    Complete structured claim and evidence

  3. Expressed human CPT2 formed medium- and long-chain acylcarnitines from acyl-CoAs; its physiological matrix-side reaction reconverts incoming acylcarnitines to acyl-CoAs plus free carnitine.

    Human carnitine palmitoyltransferase 2 / CPT2 → Palmitoyl-L-carnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and reviewed UniProt catalytic-reaction record
    experimental_model
    Human CPT2 in yeast homogenates; physiological direction from reviewed UniProt P23786/Rhea 12663.
    limitations
    The experiment directly measured the reverse reaction; direction in a cell depends on compartment and substrates.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The inner enzyme unloads the fatty-acid group and recycles carnitine.
    primary_references
    Carnitine palmitoyltransferase 2: New insights on the substrate specificity and implications for acylcarnitine profiling. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20538056/ · DOI 10.1016/j.bbadis.2010.06.002

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 106–112

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human CPT2 in yeast homogenates; physiological direction from reviewed UniProt P23786/Rhea 12663. · source_derived_draft · unverified_draft

    ## l-carnitine-cpt2-return The inner enzyme unloads the fatty-acid group and recycles carnitine. Expressed human CPT2 formed medium- and long-chain acylcarnitines from acyl-CoAs; its physiological matrix-side reaction reconverts incoming acylcarnitines to acyl-CoAs plus free carnitine. Model: Human CPT2 in yeast homogenates; physiological direction from reviewed UniProt P23786/Rhea 12663. Limitations: The experiment directly measured the reverse reaction; direction in a cell depends on compartment and substrates. Evidence access: Primary abstract and reviewed UniProt catalytic-reaction record Carnitine palmitoyltransferase 2: New insights on the substrate specificity and implications for acylcarnitine profiling. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20538056/ · DOI 10.1016/j.bbadis.2010.06.002
    Complete structured claim and evidence

  4. SELENOK supports ZDHHC6 by stabilizing the palmitoyl-ZDHHC6 acyl-enzyme intermediate.

    SELENOK → ZDHHC6 source_derived_draftsupplied_source_only
    Experimental context and source evidence
    cell_type
    · T cell
    evidence_scope
    Source-derived draft; primary-source verification required
    organism
    · Human

    Selenium in immune cells · lines 11–20

    Selenium immune-cell mechanism draft · supports · Source draft; model details require primary-source verification · source_derived_draft · unverified_draft

    # I. THE CLEANEST CHAIN — SELENOK → Ca²⁺ → NFAT → IL-2 This is the one to memorize. It's a direct, non-redox, molecule-by-molecule path from a selenium atom to a cytokine. ``` 1. Se → Sec-tRNA → SELENOK (ER membrane, single C-terminal Sec, tail in cytosol) 2. SELENOK binds ZDHHC6 (ER palmitoyl-S-acyltransferase, DHHC motif) → SELENOK is required as a COFACTOR to stabilize the palmitoyl-ZDHHC6 acyl-enzyme intermediate

    Selenium: the molecular cascade · lines 135–143

    Selenium molecular cascade draft · supports · Source draft; model details require primary-source verification · source_derived_draft · unverified_draft

    **SELENOO** — the strangest protein in the set. Its bacterial ortholog **SelO** looks exactly like a protein kinase but binds ATP **flipped backwards** in the pocket, so it transfers **AMP instead of phosphate**. It's an **AMPylase**, activated by oxidative stress, AMPylating GAPDH and other redox enzymes. A pseudokinase that runs in reverse. Human SELENOO is mitochondrial and largely uncharacterized. **MSRB1 (SELENOR)** — redox control of the cytoskeleton. **MICAL1/2** oxidizes actin **Met44 and Met47** to the R-sulfoxide → actin depolymerizes. MSRB1 reduces it back → repolymerization. In macrophages this gates phagocytic cup formation. **Selenium is a direct rheostat on actin dynamics.** Almost nobody knows this. **SELENOK** — not a peroxidase. It's the essential cofactor for **ZDHHC6**, the palmitoyl transferase. No SELENOK → failed palmitoylation of IP3R, calnexin, and others → broken Ca²⁺ flux in T cells. **Selenium regulating lipid post-translational modification.** **SELENOI (EPT1)** — the only selenoprotein with **zero redox function**. It's an ethanolamine phosphotransferase making phosphatidylethanolamine. Mutations → hereditary spastic paraplegia **SPG81**. (And PE is exactly the lipid GPX4 protects. There's a loop there worth pulling on.) **SELENON** — ER membrane, regulates **RyR1** redox state and SERCA2b. Mutations → SEPN1-related myopathy / rigid spine syndrome.
    Complete structured claim and evidence

  5. ZDHHC6 palmitoylates IP3R, producing the palmitoylated receptor state.

    ZDHHC6 → Palmitoylated IP3R source_derived_draftsupplied_source_only
    Experimental context and source evidence
    cell_type
    · T cell
    evidence_scope
    Source-derived draft; primary-source verification required
    organism
    · Human

    Selenium in immune cells · lines 22–28

    Selenium immune-cell mechanism draft · supports · Source draft; model details require primary-source verification · source_derived_draft · unverified_draft

    3. ZDHHC6 palmitoylates: • IP3R (all three isoforms) • calnexin • itself (autopalmitoylation) 4. Palmitoylated IP3R = stable, correctly localized, functional channel Non-palmitoylated IP3R = degraded / non-functional

    Selenium: the molecular cascade · lines 135–143

    Selenium molecular cascade draft · supports · Source draft; model details require primary-source verification · source_derived_draft · unverified_draft

    **SELENOO** — the strangest protein in the set. Its bacterial ortholog **SelO** looks exactly like a protein kinase but binds ATP **flipped backwards** in the pocket, so it transfers **AMP instead of phosphate**. It's an **AMPylase**, activated by oxidative stress, AMPylating GAPDH and other redox enzymes. A pseudokinase that runs in reverse. Human SELENOO is mitochondrial and largely uncharacterized. **MSRB1 (SELENOR)** — redox control of the cytoskeleton. **MICAL1/2** oxidizes actin **Met44 and Met47** to the R-sulfoxide → actin depolymerizes. MSRB1 reduces it back → repolymerization. In macrophages this gates phagocytic cup formation. **Selenium is a direct rheostat on actin dynamics.** Almost nobody knows this. **SELENOK** — not a peroxidase. It's the essential cofactor for **ZDHHC6**, the palmitoyl transferase. No SELENOK → failed palmitoylation of IP3R, calnexin, and others → broken Ca²⁺ flux in T cells. **Selenium regulating lipid post-translational modification.** **SELENOI (EPT1)** — the only selenoprotein with **zero redox function**. It's an ethanolamine phosphotransferase making phosphatidylethanolamine. Mutations → hereditary spastic paraplegia **SPG81**. (And PE is exactly the lipid GPX4 protects. There's a loop there worth pulling on.) **SELENON** — ER membrane, regulates **RyR1** redox state and SERCA2b. Mutations → SEPN1-related myopathy / rigid spine syndrome.
    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