Component

Delta-tocotrienol-13′-carboxychromanol

Delta-TE-13′-COOH; retains three side-chain double bonds and is distinct from saturated delta-tocopherol-13′-COOH.

2 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. Pein and colleagues interpreted delta-tocotrienol-13′-carboxychromanol inhibition of human 5-LO as reversible and allosteric: activity inhibition persisted when arachidonic acid was varied, and immobilized metabolite captured the enzyme despite excess arachidonic acid.

    Delta-tocotrienol-13′-carboxychromanol → Arachidonate 5-lipoxygenase (ALOX5) source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Purified human 5-LO; substrate variation, dilution and immobilized-ligand pull-down
    exposure
    Purified 5-LO 0.5 µg in PBS pH 7.4, EDTA 1 mM and ATP 1 mM; 10 min compound preincubation at 4°C, then 5–80 µM arachidonic acid and 2 mM CaCl2 at 37°C. Reported IC50 35–40 nM; pull-down competitor arachidonic acid 100 µM.
    limitations
    Binding-site assignment combines biochemical evidence with docking and mutagenesis, not a solved inhibitor-bound structure. Park 2022 explicitly disputes the noncompetitive interpretation.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Homo sapiens
    plain_language
    One study concluded that this tocotrienol metabolite inhibits 5-lipoxygenase at a site distinct from the usual fatty-acid binding site.
    primary_references
    [pein2018] Endogenous metabolites of vitamin E limit inflammation by targeting 5-lipoxygenase. (2018). https://pubmed.ncbi.nlm.nih.gov/30237488/ DOI: 10.1038/s41467-018-06158-5
    tissue_or_cell_type
    Cell-free enzyme

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 1024–1035

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human 5-LO; substrate variation, dilution and immobilized-ligand pull-down · source_derived_draft · unverified_draft

    ### e-sig-delta-te-acid-allosteric Pein and colleagues interpreted delta-tocotrienol-13′-carboxychromanol inhibition of human 5-LO as reversible and allosteric: activity inhibition persisted when arachidonic acid was varied, and immobilized metabolite captured the enzyme despite excess arachidonic acid. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: One study concluded that this tocotrienol metabolite inhibits 5-lipoxygenase at a site distinct from the usual fatty-acid binding site. organism: Homo sapiens tissue_or_cell_type: Cell-free enzyme experimental_model: Purified human 5-LO; substrate variation, dilution and immobilized-ligand pull-down limitations: Binding-site assignment combines biochemical evidence with docking and mutagenesis, not a solved inhibitor-bound structure. Park 2022 explicitly disputes the noncompetitive interpretation. exposure: Purified 5-LO 0.5 µg in PBS pH 7.4, EDTA 1 mM and ATP 1 mM; 10 min compound preincubation at 4°C, then 5–80 µM arachidonic acid and 2 mM CaCl2 at 37°C. Reported IC50 35–40 nM; pull-down competitor arachidonic acid 100 µM. cross_nutrient: false [pein2018] Endogenous metabolites of vitamin E limit inflammation by targeting 5-lipoxygenase. (2018). https://pubmed.ncbi.nlm.nih.gov/30237488/ DOI: 10.1038/s41467-018-06158-5
    Complete structured claim and evidence

  2. Park and colleagues classified Delta-tocotrienol-13′-carboxychromanol as a competitive inhibitor of human recombinant 5-LOX, with Ki 0.8 µM; oxygen-consumption kinetics showed increased apparent substrate requirement without an apparent decrease in Vmax.

    Delta-tocotrienol-13′-carboxychromanol → Arachidonate 5-lipoxygenase (ALOX5) source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Human recombinant 5-LOX oxygen-electrode initial-rate kinetics
    exposure
    10 min inhibitor preincubation; arachidonic acid 5–50 µM in 50 mM Tris pH 7.4 and 0.4 mM CaCl2; reported substrate Km 2.1 µM.
    limitations
    Kinetic classification is not a solved binding structure. The delta-tocotrienol metabolite result conflicts with Pein’s allosteric interpretation; differing IC50 values alone are not treated as conflicts.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Homo sapiens
    plain_language
    Kinetic measurements in this study indicated competition between this compound and arachidonic acid at 5-lipoxygenase.
    primary_references
    [park2022] Different forms of vitamin E and metabolite 13'-carboxychromanols inhibit cyclooxygenase-1 and its catalyzed thromboxane in platelets, and tocotrienols and 13'-carboxychromanols are competitive inhibitors of 5-lipoxygenase. (2022). https://pubmed.ncbi.nlm.nih.gov/34710615/ DOI: 10.1016/j.jnutbio.2021.108884
    tissue_or_cell_type
    Cell-free enzyme

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 1037–1048

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human recombinant 5-LOX oxygen-electrode initial-rate kinetics · source_derived_draft · unverified_draft

    ### e-sig-delta-te-acid-competitive Park and colleagues classified Delta-tocotrienol-13′-carboxychromanol as a competitive inhibitor of human recombinant 5-LOX, with Ki 0.8 µM; oxygen-consumption kinetics showed increased apparent substrate requirement without an apparent decrease in Vmax. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Kinetic measurements in this study indicated competition between this compound and arachidonic acid at 5-lipoxygenase. organism: Homo sapiens tissue_or_cell_type: Cell-free enzyme experimental_model: Human recombinant 5-LOX oxygen-electrode initial-rate kinetics limitations: Kinetic classification is not a solved binding structure. The delta-tocotrienol metabolite result conflicts with Pein’s allosteric interpretation; differing IC50 values alone are not treated as conflicts. exposure: 10 min inhibitor preincubation; arachidonic acid 5–50 µM in 50 mM Tris pH 7.4 and 0.4 mM CaCl2; reported substrate Km 2.1 µM. cross_nutrient: false [park2022] Different forms of vitamin E and metabolite 13'-carboxychromanols inhibit cyclooxygenase-1 and its catalyzed thromboxane in platelets, and tocotrienols and 13'-carboxychromanols are competitive inhibitors of 5-lipoxygenase. (2022). https://pubmed.ncbi.nlm.nih.gov/34710615/ DOI: 10.1016/j.jnutbio.2021.108884
    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