Component

Human cytochrome P450 4F2

Human CYP4F2 protein; tested directly for tocopherol and phylloquinone hydroxylation.

6 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. CYP4F2, but not CYP4F11, supported sequential MK-4 oxidation to the omega-acid without apparent release of the aldehyde intermediate.

    Human cytochrome P450 4F2 → Menaquinone-4 omega-carboxylic acid source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/24138531.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb", "start_char": 0, "end_char": 1608, "text_sha256": "bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb"}
    experimental_model
    Purified enzymes, liver microsomes and genotyping
    exposure
    MK-4 oxidation and common enzyme variants
    limitations
    Catabolism assay; no assumption that all long-chain menaquinones have identical kinetics.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Human CYP4F2/CYP4F11 and human liver microsomes
    plain_language
    The two enzymes did not perform every later breakdown step equally.
    primary_references
    [k2-p24138531] Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. (2013). https://pubmed.ncbi.nlm.nih.gov/24138531/ DOI: 10.1021/bi401208m
    tissue_or_cell_type
    MK-4 catabolism

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 344–355

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified enzymes, liver microsomes and genotyping · source_derived_draft · unverified_draft

    ### k2-cyp4f2-acid CYP4F2, but not CYP4F11, supported sequential MK-4 oxidation to the omega-acid without apparent release of the aldehyde intermediate. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The two enzymes did not perform every later breakdown step equally. organism: Human CYP4F2/CYP4F11 and human liver microsomes tissue_or_cell_type: MK-4 catabolism experimental_model: Purified enzymes, liver microsomes and genotyping limitations: Catabolism assay; no assumption that all long-chain menaquinones have identical kinetics. exposure: MK-4 oxidation and common enzyme variants evidence_span: {"source_cache": "artifacts/k2-research/24138531.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb", "start_char": 0, "end_char": 1608, "text_sha256": "bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb"} [k2-p24138531] Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. (2013). https://pubmed.ncbi.nlm.nih.gov/24138531/ DOI: 10.1021/bi401208m
    Complete structured claim and evidence

  2. Purified CYP4F2 catalyzed MK-4 terminal side-chain hydroxylation in vitro.

    Human cytochrome P450 4F2 → Menaquinone-4 / MK-4 / menatetrenone source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/k2-research/24138531.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb", "start_char": 0, "end_char": 1608, "text_sha256": "bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb"}
    experimental_model
    Purified enzymes, liver microsomes and genotyping
    exposure
    MK-4 oxidation and common enzyme variants
    limitations
    Catabolism assay; no assumption that all long-chain menaquinones have identical kinetics.
    nutrient_topic
    Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
    organism
    Human CYP4F2/CYP4F11 and human liver microsomes
    plain_language
    An enzyme begins breaking down MK-4 by modifying the end of its side chain.
    primary_references
    [k2-p24138531] Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. (2013). https://pubmed.ncbi.nlm.nih.gov/24138531/ DOI: 10.1021/bi401208m
    tissue_or_cell_type
    MK-4 catabolism

    Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 318–329

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified enzymes, liver microsomes and genotyping · source_derived_draft · unverified_draft

    ### k2-cyp4f2-mk4 Purified CYP4F2 catalyzed MK-4 terminal side-chain hydroxylation in vitro. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: An enzyme begins breaking down MK-4 by modifying the end of its side chain. organism: Human CYP4F2/CYP4F11 and human liver microsomes tissue_or_cell_type: MK-4 catabolism experimental_model: Purified enzymes, liver microsomes and genotyping limitations: Catabolism assay; no assumption that all long-chain menaquinones have identical kinetics. exposure: MK-4 oxidation and common enzyme variants evidence_span: {"source_cache": "artifacts/k2-research/24138531.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb", "start_char": 0, "end_char": 1608, "text_sha256": "bcb3784026ddabfeb55257cddc84ffd1001d6eb4fb04ba2e9daf8ade8de770fb"} [k2-p24138531] Cytochrome P450-dependent catabolism of vitamin K: ω-hydroxylation catalyzed by human CYP4F2 and CYP4F11. (2013). https://pubmed.ncbi.nlm.nih.gov/24138531/ DOI: 10.1021/bi401208m
    Complete structured claim and evidence

  3. Recombinant human CYP4F2 catalyzed terminal side-chain hydroxylation of alpha-tocopherol to its 13′-hydroxy product.

    Human cytochrome P450 4F2 → 13′-Hydroxy-alpha-tocopherol source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Recombinant human P450 enzyme comparison
    exposure
    alpha-Tocopherol substrate with NADPH; quantitative incubation details not assigned here.
    limitations
    Initial oxidation only; other enzymes perform subsequent side-chain shortening.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Human protein in recombinant microsomes
    plain_language
    CYP4F2 begins breakdown of this tocopherol form.
    primary_references
    [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
    tissue_or_cell_type
    Microsomal enzyme preparation

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 402–413

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human P450 enzyme comparison · source_derived_draft · unverified_draft

    ### ve-transport-cyp4f2-alpha-hydroxylation Recombinant human CYP4F2 catalyzed terminal side-chain hydroxylation of alpha-tocopherol to its 13′-hydroxy product. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: CYP4F2 begins breakdown of this tocopherol form. organism: Human protein in recombinant microsomes tissue_or_cell_type: Microsomal enzyme preparation experimental_model: Recombinant human P450 enzyme comparison limitations: Initial oxidation only; other enzymes perform subsequent side-chain shortening. exposure: alpha-Tocopherol substrate with NADPH; quantitative incubation details not assigned here. cross_nutrient: false [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
    Complete structured claim and evidence

  4. Recombinant human CYP4F2 catalyzed terminal side-chain hydroxylation of gamma-tocopherol to its 13′-hydroxy product.

    Human cytochrome P450 4F2 → 13′-Hydroxy-gamma-tocopherol source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Recombinant human P450 enzyme comparison
    exposure
    gamma-Tocopherol substrate with NADPH; quantitative incubation details not assigned here.
    limitations
    Initial oxidation only; other enzymes perform subsequent side-chain shortening.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Human protein in recombinant microsomes
    plain_language
    CYP4F2 begins breakdown of this tocopherol form.
    primary_references
    [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
    tissue_or_cell_type
    Microsomal enzyme preparation

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 415–426

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human P450 enzyme comparison · source_derived_draft · unverified_draft

    ### ve-transport-cyp4f2-gamma-hydroxylation Recombinant human CYP4F2 catalyzed terminal side-chain hydroxylation of gamma-tocopherol to its 13′-hydroxy product. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: CYP4F2 begins breakdown of this tocopherol form. organism: Human protein in recombinant microsomes tissue_or_cell_type: Microsomal enzyme preparation experimental_model: Recombinant human P450 enzyme comparison limitations: Initial oxidation only; other enzymes perform subsequent side-chain shortening. exposure: gamma-Tocopherol substrate with NADPH; quantitative incubation details not assigned here. cross_nutrient: false [sontag2002] Cytochrome P450 omega-hydroxylase pathway of tocopherol catabolism. Novel mechanism of regulation of vitamin E status. (2002). https://pubmed.ncbi.nlm.nih.gov/11997390/ DOI: 10.1074/jbc.m201466200
    Complete structured claim and evidence

  5. Human CYP4F2-expressing microsomes hydroxylated phylloquinone, demonstrating substrate overlap with tocopherol catabolism.

    Human cytochrome P450 4F2 → Omega-hydroxyphylloquinone source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Recombinant CYP4F2 kinetic assay
    exposure
    25 pmol CYP4F2; labeled phylloquinone 1–100 µM; 1 mM NADPH; 30 min at 37 °C.
    limitations
    Shared substrate use alone does not imply vitamin E accelerates vitamin K depletion.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Human protein in insect microsomes
    plain_language
    Vitamins E and K1 share an initial catabolic enzyme.
    primary_references
    [farley2013] ω-Hydroxylation of phylloquinone by CYP4F2 is not increased by α-tocopherol. (2013). https://pubmed.ncbi.nlm.nih.gov/23650179/ DOI: 10.1002/mnfr.201200797
    tissue_or_cell_type
    Microsomal enzyme preparation

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 454–465

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant CYP4F2 kinetic assay · source_derived_draft · unverified_draft

    ### ve-transport-cyp4f2-k1-hydroxylation Human CYP4F2-expressing microsomes hydroxylated phylloquinone, demonstrating substrate overlap with tocopherol catabolism. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamins E and K1 share an initial catabolic enzyme. organism: Human protein in insect microsomes tissue_or_cell_type: Microsomal enzyme preparation experimental_model: Recombinant CYP4F2 kinetic assay limitations: Shared substrate use alone does not imply vitamin E accelerates vitamin K depletion. exposure: 25 pmol CYP4F2; labeled phylloquinone 1–100 µM; 1 mM NADPH; 30 min at 37 °C. cross_nutrient: true [farley2013] ω-Hydroxylation of phylloquinone by CYP4F2 is not increased by α-tocopherol. (2013). https://pubmed.ncbi.nlm.nih.gov/23650179/ DOI: 10.1002/mnfr.201200797
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Alpha-tocopherol did not increase phylloquinone omega-hydroxylation in CYP4F2 microsomes; the study reported a slight decrease in apparent phylloquinone Vmax.

    RRR-alpha-tocopherol → CYP4F2-mediated phylloquinone omega-hydroxylation source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    true
    experimental_model
    Recombinant human CYP4F2 co-substrate kinetics
    exposure
    Labeled phylloquinone 0–50 µM with RRR-alpha-tocopherol 0–50 µM or SRR-alpha-tocopherol 0–100 µM; 30 min, 37 °C, 1 mM NADPH.
    limitations
    Does not exclude other mechanisms of vitamin E–K interaction in animals or humans.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Human protein in insect microsomes
    plain_language
    This assay did not support faster vitamin K1 breakdown caused by alpha-tocopherol.
    primary_references
    [farley2013] ω-Hydroxylation of phylloquinone by CYP4F2 is not increased by α-tocopherol. (2013). https://pubmed.ncbi.nlm.nih.gov/23650179/ DOI: 10.1002/mnfr.201200797
    tissue_or_cell_type
    Microsomal enzyme preparation

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 467–478

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human CYP4F2 co-substrate kinetics · source_derived_draft · unverified_draft

    ### ve-transport-alpha-does-not-activate-k1-catabolism Alpha-tocopherol did not increase phylloquinone omega-hydroxylation in CYP4F2 microsomes; the study reported a slight decrease in apparent phylloquinone Vmax. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: This assay did not support faster vitamin K1 breakdown caused by alpha-tocopherol. organism: Human protein in insect microsomes tissue_or_cell_type: Microsomal enzyme preparation experimental_model: Recombinant human CYP4F2 co-substrate kinetics limitations: Does not exclude other mechanisms of vitamin E–K interaction in animals or humans. exposure: Labeled phylloquinone 0–50 µM with RRR-alpha-tocopherol 0–50 µM or SRR-alpha-tocopherol 0–100 µM; 30 min, 37 °C, 1 mM NADPH. cross_nutrient: true [farley2013] ω-Hydroxylation of phylloquinone by CYP4F2 is not increased by α-tocopherol. (2013). https://pubmed.ncbi.nlm.nih.gov/23650179/ DOI: 10.1002/mnfr.201200797
    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