Gamma-glutamyl carboxylase / GGCX

cross_nutrient

Vitamin D regulates osteocalcin expression in specified models; vitamin K-dependent carboxylation modifies its protein product through a distinct enzyme reaction.

evidence_locator

Abstract: reported experimental results

evidence_scope

D3 active metabolite or VDR machinery experiment; not a direct D2-versus-D3 comparison.

experimental_model

Microsomal vitamin K-dependent carboxylase enriched about 100-fold; bovine osteocalcin substrate and CO2-incorporation assay

exposure

50 mM bicarbonate, excess enriched carboxylase and limiting decarboxylated osteocalcin; vitamin K-dependent reaction conditions.

limitations

In-vitro modification of a defined substrate; no D-plus-K supplementation regimen, K2-specific necessity, improved fracture outcome or obligatory supplement pairing was tested.

nutrient

Vitamin D2 and D3 · Vitamin D2 and D3

nutrient_topic

Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin D2 and D3

organism

Bos taurus osteocalcin; liver-derived enzyme preparation

plain_language

Osteocalcin needs a separate vitamin K-dependent protein-modification step; making more osteocalcin is not the same reaction.

primary_references

[vdm-soute1987] Vitamin K-dependent carboxylase: increased efficiency of the carboxylation reaction. (1987). https://pubmed.ncbi.nlm.nih.gov/3495900/ DOI: 10.1055/s-0038-1651066

tissue_or_cell_type

Cell-free enzyme assay

Vitamin D2 and D3: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 889–903

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Microsomal vitamin K-dependent carboxylase enriched about 100-fold; bovine osteocalcin substrate and CO2-incorporation assay · source_derived_draft · unverified_draft

### vdm-vitamin-k-carboxylase-modifies-osteocalcin A concentrated vitamin K-dependent carboxylase preparation converted glutamate residues of decarboxylated bovine osteocalcin into gamma-carboxyglutamate in vitro. Condition category: normal nutrient_topic: Vitamin D2 and D3 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Osteocalcin needs a separate vitamin K-dependent protein-modification step; making more osteocalcin is not the same reaction. organism: Bos taurus osteocalcin; liver-derived enzyme preparation tissue_or_cell_type: Cell-free enzyme assay experimental_model: Microsomal vitamin K-dependent carboxylase enriched about 100-fold; bovine osteocalcin substrate and CO2-incorporation assay limitations: In-vitro modification of a defined substrate; no D-plus-K supplementation regimen, K2-specific necessity, improved fracture outcome or obligatory supplement pairing was tested. exposure: 50 mM bicarbonate, excess enriched carboxylase and limiting decarboxylated osteocalcin; vitamin K-dependent reaction conditions. cross_nutrient: Vitamin D regulates osteocalcin expression in specified models; vitamin K-dependent carboxylation modifies its protein product through a distinct enzyme reaction. evidence_locator: Abstract: reported experimental results nutrient: Vitamin D2 and D3 evidence_scope: D3 active metabolite or VDR machinery experiment; not a direct D2-versus-D3 comparison. [vdm-soute1987] Vitamin K-dependent carboxylase: increased efficiency of the carboxylation reaction. (1987). https://pubmed.ncbi.nlm.nih.gov/3495900/ DOI: 10.1055/s-0038-1651066

evidence_span

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experimental_model

Cryo-EM, mutagenesis and molecular dynamics

exposure

GGCX complexes with vitamin K, clotting-factor substrates and osteocalcin

limitations

The carbon-capture/proton-transfer sequence is the authors' structural mechanistic model, not a measured human dietary response or an established bicarbonate-supplement interaction.

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

The added chemical group comes from carbon dioxide; vitamin K supports the reaction rather than supplying the carbon.

primary_references

[k2-p41290650] Structural insight into bicarbonate-mediated carboxylation by human vitamin K-dependent carboxylase. (2025). https://pubmed.ncbi.nlm.nih.gov/41290650/ DOI: 10.1038/s41467-025-65488-3

tissue_or_cell_type

Substrate recognition and carbon-dioxide capture

Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 422–433

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM, mutagenesis and molecular dynamics · source_derived_draft · unverified_draft

### k2-ggcx-carbon-capture Cryo-EM structures and biochemical analyses supported a proposed bicarbonate-mediated carbon-dioxide capture model for GGCX. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The added chemical group comes from carbon dioxide; vitamin K supports the reaction rather than supplying the carbon. organism: Human GGCX tissue_or_cell_type: Substrate recognition and carbon-dioxide capture experimental_model: Cryo-EM, mutagenesis and molecular dynamics limitations: The carbon-capture/proton-transfer sequence is the authors' structural mechanistic model, not a measured human dietary response or an established bicarbonate-supplement interaction. exposure: GGCX complexes with vitamin K, clotting-factor substrates and osteocalcin evidence_span: {"source_cache": "artifacts/k2-research/41290650.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0ea90e4c1af519fa0fc3645f4a4f8f0721924797e0eaa44569ff445c4afe19bc", "start_char": 0, "end_char": 1177, "text_sha256": "0ea90e4c1af519fa0fc3645f4a4f8f0721924797e0eaa44569ff445c4afe19bc"} [k2-p41290650] Structural insight into bicarbonate-mediated carboxylation by human vitamin K-dependent carboxylase. (2025). https://pubmed.ncbi.nlm.nih.gov/41290650/ DOI: 10.1038/s41467-025-65488-3

evidence_span

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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

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

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experimental_model

Human compound-heterozygous GGCX case and mutation analysis

exposure

Splice-site and Arg485Pro variants; vitamin K substitution

limitations

Single rare genetic case; the suspected binding-site mechanism was proposed, not established by structure.

nutrient_topic

Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family

organism

Human patient

plain_language

The nutrient cannot necessarily repair the protein that uses it.

primary_references

[k2-p15287948] Compound heterozygous mutations in the gamma-glutamyl carboxylase gene cause combined deficiency of all vitamin K-dependent blood coagulation factors. (2004). https://pubmed.ncbi.nlm.nih.gov/15287948/ DOI: 10.1111/j.1365-2141.2004.05071.x

tissue_or_cell_type

Vitamin K-dependent coagulation proteins

trigger_kind

machinery_impairment Imported condition classification; unverified.

Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 929–940

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human compound-heterozygous GGCX case and mutation analysis · source_derived_draft · unverified_draft

### k2-ggcx-factor-defect The GGCX case had combined vitamin K-dependent factor deficiency; vitamin K substitution only partly normalized factor levels. Condition category: machinery_impairment nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The nutrient cannot necessarily repair the protein that uses it. organism: Human patient tissue_or_cell_type: Vitamin K-dependent coagulation proteins experimental_model: Human compound-heterozygous GGCX case and mutation analysis limitations: Single rare genetic case; the suspected binding-site mechanism was proposed, not established by structure. exposure: Splice-site and Arg485Pro variants; vitamin K substitution evidence_span: {"source_cache": "artifacts/k2-research/15287948.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "76e5cf58ebc717968ad3ae32a76aec9f05e783468666181042dfb8989805dadf", "start_char": 0, "end_char": 1069, "text_sha256": "76e5cf58ebc717968ad3ae32a76aec9f05e783468666181042dfb8989805dadf"} [k2-p15287948] Compound heterozygous mutations in the gamma-glutamyl carboxylase gene cause combined deficiency of all vitamin K-dependent blood coagulation factors. (2004). https://pubmed.ncbi.nlm.nih.gov/15287948/ DOI: 10.1111/j.1365-2141.2004.05071.x

evidence_span

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experimental_model

Cryo-EM, mutagenesis and molecular dynamics

exposure

GGCX complexes with vitamin K, clotting-factor substrates and osteocalcin

limitations

Structural and biochemical model; the proposed bicarbonate proton relay is not a demonstrated benefit of bicarbonate ingestion.

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

The enzyme can modify several sites on the same protein during one encounter.

primary_references

[k2-p41290650] Structural insight into bicarbonate-mediated carboxylation by human vitamin K-dependent carboxylase. (2025). https://pubmed.ncbi.nlm.nih.gov/41290650/ DOI: 10.1038/s41467-025-65488-3

tissue_or_cell_type

Substrate recognition and carbon-dioxide capture

Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 409–420

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM, mutagenesis and molecular dynamics · source_derived_draft · unverified_draft

### k2-ggcx-processivity A conserved dipeptide-anchoring mechanism supports repeated glutamate carboxylation while a substrate remains associated with GGCX. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The enzyme can modify several sites on the same protein during one encounter. organism: Human GGCX tissue_or_cell_type: Substrate recognition and carbon-dioxide capture experimental_model: Cryo-EM, mutagenesis and molecular dynamics limitations: Structural and biochemical model; the proposed bicarbonate proton relay is not a demonstrated benefit of bicarbonate ingestion. exposure: GGCX complexes with vitamin K, clotting-factor substrates and osteocalcin evidence_span: {"source_cache": "artifacts/k2-research/41290650.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0ea90e4c1af519fa0fc3645f4a4f8f0721924797e0eaa44569ff445c4afe19bc", "start_char": 0, "end_char": 1177, "text_sha256": "0ea90e4c1af519fa0fc3645f4a4f8f0721924797e0eaa44569ff445c4afe19bc"} [k2-p41290650] Structural insight into bicarbonate-mediated carboxylation by human vitamin K-dependent carboxylase. (2025). https://pubmed.ncbi.nlm.nih.gov/41290650/ DOI: 10.1038/s41467-025-65488-3

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

Membrane cholesterol is part of the enzyme environment, not just an unrelated blood measurement.

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 396–407

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-cholesterol A cholesterol molecule interacted with GGCX transmembrane helices; structural, cellular and simulation results connected this site with regulation of cellular GGCX protein levels. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Membrane cholesterol is part of the enzyme environment, not just an unrelated blood measurement. 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

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

The target protein helps organize the enzyme that modifies it.

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 383–394

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-osteocalcin-binding Vitamin K-dependent protein propeptide binding stabilized GGCX transmembrane helices 6 and 7 and created its vitamin-K-binding pocket. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The target protein helps organize the enzyme that modifies it. 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

evidence_span

{"source_cache": "artifacts/k2-research/36788244.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5fda09197d386351a1b1d261c9b385db36e02eab0c238bf18599d7086b501f93", "start_char": 0, "end_char": 1359, "text_sha256": "5fda09197d386351a1b1d261c9b385db36e02eab0c238bf18599d7086b501f93"}

experimental_model

Genome-wide CRISPR screen and reporter biochemistry

exposure

FSP1 knockout/inhibition and DHODH comparison

limitations

Supports cycle biochemistry; a different ferroptosis defense enzyme need not share the same vitamin K function.

nutrient_topic

Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin K2 / menaquinone family

organism

Human vitamin K-dependent reporter cells

plain_language

The antioxidant enzyme also helps supply cofactor for protein modification.

primary_references

[k2-p36788244] A genome-wide CRISPR-Cas9 knockout screen identifies FSP1 as the warfarin-resistant vitamin K reductase. (2023). https://pubmed.ncbi.nlm.nih.gov/36788244/ DOI: 10.1038/s41467-023-36446-8

tissue_or_cell_type

Warfarin-resistant quinone reduction

Vitamin K2: menaquinone forms, carboxylation, recycling and nutrient interactions (2026-09-17) · lines 825–836

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Genome-wide CRISPR screen and reporter biochemistry · source_derived_draft · unverified_draft

### k2-fsp1-carboxylation A CRISPR screen independently identified FSP1 as the warfarin-resistant vitamin K reductase; FSP1 inhibition impaired vitamin K-dependent carboxylation. Condition category: normal nutrient_topic: Vitamin K2 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The antioxidant enzyme also helps supply cofactor for protein modification. organism: Human vitamin K-dependent reporter cells tissue_or_cell_type: Warfarin-resistant quinone reduction experimental_model: Genome-wide CRISPR screen and reporter biochemistry limitations: Supports cycle biochemistry; a different ferroptosis defense enzyme need not share the same vitamin K function. exposure: FSP1 knockout/inhibition and DHODH comparison evidence_span: {"source_cache": "artifacts/k2-research/36788244.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "5fda09197d386351a1b1d261c9b385db36e02eab0c238bf18599d7086b501f93", "start_char": 0, "end_char": 1359, "text_sha256": "5fda09197d386351a1b1d261c9b385db36e02eab0c238bf18599d7086b501f93"} [k2-p36788244] A genome-wide CRISPR-Cas9 knockout screen identifies FSP1 as the warfarin-resistant vitamin K reductase. (2023). https://pubmed.ncbi.nlm.nih.gov/36788244/ DOI: 10.1038/s41467-023-36446-8