Vitamin K 2,3-epoxide family: molecular mechanisms & dependencies

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.

Human evidence only

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)

GGCX couples oxidation of reduced vitamin K to conversion of protein-bound glutamate into gamma-carboxyglutamate.
Gamma-glutamyl carboxylase / GGCX → Reduced vitamin K hydroquinone family source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/k2-research/39880952.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "eb8e6d00eecd7c5c780921cae3f804fab60e919301eeb16e9909f36293aaa653", "start_char": 0, "end_char": 1230, "text_sha256": "eb8e6d00eecd7c5c780921cae3f804fab60e919301eeb16e9909f36293aaa653"}
experimental_model
Cryo-EM, binding, cell assays and molecular dynamics
exposure
Apo, osteocalcin-bound and vitamin-K-bound structures
limitations
Shared vitamin K chemistry; the abstract does not establish K2 exclusivity or identical kinetics for every menaquinone.
nutrient_topic
Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
organism
Human GGCX
plain_language
Vitamin K helps an enzyme modify selected proteins; it does not carry calcium into bone itself.
primary_references
[k2-p39880952] Structure and mechanism of vitamin-K-dependent γ-glutamyl carboxylase. (2025). https://pubmed.ncbi.nlm.nih.gov/39880952/ DOI: 10.1038/s41586-024-08484-9
tissue_or_cell_type
Endoplasmic-reticulum membrane enzyme
Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 370–381
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM, binding, cell assays and molecular dynamics · source_derived_draft · unverified_draft
### k2-ggcx-cofactor GGCX couples oxidation of reduced vitamin K to conversion of protein-bound glutamate into gamma-carboxyglutamate. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Vitamin K helps an enzyme modify selected proteins; it does not carry calcium into bone itself. organism: Human GGCX tissue_or_cell_type: Endoplasmic-reticulum membrane enzyme experimental_model: Cryo-EM, binding, cell assays and molecular dynamics limitations: Shared vitamin K chemistry; the abstract does not establish K2 exclusivity or identical kinetics for every menaquinone. exposure: Apo, osteocalcin-bound and vitamin-K-bound structures evidence_span: {"source_cache": "artifacts/k2-research/39880952.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "eb8e6d00eecd7c5c780921cae3f804fab60e919301eeb16e9909f36293aaa653", "start_char": 0, "end_char": 1230, "text_sha256": "eb8e6d00eecd7c5c780921cae3f804fab60e919301eeb16e9909f36293aaa653"} [k2-p39880952] Structure and mechanism of vitamin-K-dependent γ-glutamyl carboxylase. (2025). https://pubmed.ncbi.nlm.nih.gov/39880952/ DOI: 10.1038/s41586-024-08484-9
Complete structured claim and evidence
Silencing the identified VKORC1 gene reduced vitamin K epoxide reductase activity; recombinant expression restored warfarin-sensitive enzyme activity.
Human vitamin K epoxide reductase / VKORC1 → Vitamin K epoxide recycling source_derived_draftungraded
Experimental context and source evidence
evidence_span
{"source_cache": "artifacts/k2-research/14765195.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "32f373fc0363ed079e580b2d47a3cb36c82b46871860fc6740b0285e23936496", "start_char": 0, "end_char": 1385, "text_sha256": "32f373fc0363ed079e580b2d47a3cb36c82b46871860fc6740b0285e23936496"}
experimental_model
siRNA identification and recombinant expression
exposure
Gene silencing, enzyme expression and warfarin sensitivity
limitations
Gene-discovery experiments; later structural understanding supersedes the original minimal topology description.
nutrient_topic
Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family
organism
Human VKORC1 and insect-cell expression
plain_language
The used vitamin K cofactor can be recycled instead of being replaced after every reaction.
primary_references
[k2-p14765195] Identification of the gene for vitamin K epoxide reductase. (2004). https://pubmed.ncbi.nlm.nih.gov/14765195/ DOI: 10.1038/nature02254
tissue_or_cell_type
Vitamin K recycling enzyme
Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 435–446
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · siRNA identification and recombinant expression · source_derived_draft · unverified_draft
### k2-vkor-recycling Silencing the identified VKORC1 gene reduced vitamin K epoxide reductase activity; recombinant expression restored warfarin-sensitive enzyme activity. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The used vitamin K cofactor can be recycled instead of being replaced after every reaction. organism: Human VKORC1 and insect-cell expression tissue_or_cell_type: Vitamin K recycling enzyme experimental_model: siRNA identification and recombinant expression limitations: Gene-discovery experiments; later structural understanding supersedes the original minimal topology description. exposure: Gene silencing, enzyme expression and warfarin sensitivity evidence_span: {"source_cache": "artifacts/k2-research/14765195.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "32f373fc0363ed079e580b2d47a3cb36c82b46871860fc6740b0285e23936496", "start_char": 0, "end_char": 1385, "text_sha256": "32f373fc0363ed079e580b2d47a3cb36c82b46871860fc6740b0285e23936496"} [k2-p14765195] Identification of the gene for vitamin K epoxide reductase. (2004). https://pubmed.ncbi.nlm.nih.gov/14765195/ DOI: 10.1038/nature02254
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.

Vitamin K 2,3-epoxide family