Component
Human cytochrome P450 4F11
Human cytochrome P450 4F11. Species, exposure and limitations are retained in each linked 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
Purified CYP4F11 catalyzed MK-4 terminal side-chain hydroxylation in vitro.
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 331–342
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-cyp4f11-mk4 Purified CYP4F11 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
Where it participates (unsigned role)
CYP4F2, but not CYP4F11, supported sequential MK-4 oxidation to the omega-acid without apparent release of the aldehyde intermediate.
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
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.