Component

Glucose-6-phosphate dehydrogenase / G6PD

Measured process or biological entity; consult each linked claim for the experimental scope.

7 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. In G6PD-deficient erythrocytes, glutathione reductase was usually already FAD-saturated despite evidence of low FMN-dependent oxidase activity.

    Glucose-6-phosphate dehydrogenase / G6PD → Erythrocyte glutathione reductase activation coefficient / EGRAC source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    cross_nutrient
    G6PD genotype and distinct flavin pools alter interpretation of B2/B6-linked assays.
    experimental_model
    Human erythrocytes from G6PD deficiency, heterozygous beta-thalassemia and controls.
    exposure
    In-vitro FAD stimulation of glutathione reductase and PNP oxidase activity, with oral-riboflavin response observations.
    limitations
    Human red-cell observation; the proposed faster FMN-to-FAD flux was an interpretation, not a directly measured universal mechanism.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Homo sapiens
    plain_language
    A red-cell FAD saturation test can look adequate while another B2-dependent enzyme system is poorly supplied.
    primary_references
    [b2-anderson1987] Glutathione reductase activity and its relationship to pyridoxine phosphate activity in G6PD deficiency (1987). https://pubmed.ncbi.nlm.nih.gov/3582603/ DOI: 10.1111/j.1600-0609.1987.tb01417.x
    tissue_or_cell_type
    Human clinical setting
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1666–1677

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human erythrocytes from G6PD deficiency, heterozygous beta-thalassemia and controls. · source_derived_draft · unverified_draft

    ### b2-g6pd-fad-assay-limit In G6PD-deficient erythrocytes, glutathione reductase was usually already FAD-saturated despite evidence of low FMN-dependent oxidase activity. Condition category: biomarker_context nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A red-cell FAD saturation test can look adequate while another B2-dependent enzyme system is poorly supplied. organism: Homo sapiens tissue_or_cell_type: Human clinical setting experimental_model: Human erythrocytes from G6PD deficiency, heterozygous beta-thalassemia and controls. limitations: Human red-cell observation; the proposed faster FMN-to-FAD flux was an interpretation, not a directly measured universal mechanism. exposure: In-vitro FAD stimulation of glutathione reductase and PNP oxidase activity, with oral-riboflavin response observations. cross_nutrient: G6PD genotype and distinct flavin pools alter interpretation of B2/B6-linked assays. [b2-anderson1987] Glutathione reductase activity and its relationship to pyridoxine phosphate activity in G6PD deficiency (1987). https://pubmed.ncbi.nlm.nih.gov/3582603/ DOI: 10.1111/j.1600-0609.1987.tb01417.x
    Complete structured claim and evidence

  2. Erythrocytes from a G6PD-deficient person failed to reduce lipoic acid in the assay; pharmacological G6PD inhibition also prevented reduction.

    Glucose-6-phosphate dehydrogenase / G6PD → Erythrocyte reduction of free lipoic acid source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/ala-research/7632170.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707", "start_char": 0, "end_char": 1863, "text_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707"}
    experimental_model
    Human erythrocytes, one G6PD-deficient donor and purified-enzyme assays
    exposure
    Lipoic acid with glucose/2-deoxyglucose and G6PD inhibition
    limitations
    The deficient-donor finding is small and mechanistic; it is not a clinical safety or efficacy trial in G6PD deficiency.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human
    plain_language
    Providing the oxidized molecule did not overcome the missing reducing capacity.
    primary_references
    [ala-p7632170] Reduction and transport of lipoic acid by human erythrocytes. (1995). https://pubmed.ncbi.nlm.nih.gov/7632170/ DOI: 10.1016/0006-2952(95)00084-d
    tissue_or_cell_type
    Erythrocytes and glutathione reductase
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 728–739

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human erythrocytes, one G6PD-deficient donor and purified-enzyme assays · source_derived_draft · unverified_draft

    ### ala-g6pd-reduction-failure Erythrocytes from a G6PD-deficient person failed to reduce lipoic acid in the assay; pharmacological G6PD inhibition also prevented reduction. Condition category: machinery_impairment nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: Providing the oxidized molecule did not overcome the missing reducing capacity. organism: Human tissue_or_cell_type: Erythrocytes and glutathione reductase experimental_model: Human erythrocytes, one G6PD-deficient donor and purified-enzyme assays limitations: The deficient-donor finding is small and mechanistic; it is not a clinical safety or efficacy trial in G6PD deficiency. exposure: Lipoic acid with glucose/2-deoxyglucose and G6PD inhibition evidence_span: {"source_cache": "artifacts/ala-research/7632170.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707", "start_char": 0, "end_char": 1863, "text_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707"} [ala-p7632170] Reduction and transport of lipoic acid by human erythrocytes. (1995). https://pubmed.ncbi.nlm.nih.gov/7632170/ DOI: 10.1016/0006-2952(95)00084-d
    Complete structured claim and evidence

  3. Human G6PD uses glucose-6-phosphate and catalytic NADP+ to generate NADPH.

    Glucose-6-phosphate dehydrogenase / G6PD → NADPH source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/35858355.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "02c2d0e880b17ab304fab0854064813ffec5fa9e647b978a083aa88fbf8a38f0", "start_char": 0, "end_char": 1328, "text_sha256": "02c2d0e880b17ab304fab0854064813ffec5fa9e647b978a083aa88fbf8a38f0"}
    experimental_model
    Cryo-EM and structural comparison
    exposure
    Ligand-free and NADP/G6P-bound states
    limitations
    Structural NADP and catalytic NADP are different sites; enzyme activity is not a niacin-treatment trial.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human
    plain_language
    The reducing power used in glutathione recycling has to be replenished.
    primary_references
    [glutathione-p35858355] Allosteric role of a structural NADP+ molecule in glucose-6-phosphate dehydrogenase activity. (2022). https://pubmed.ncbi.nlm.nih.gov/35858355/ DOI: 10.1073/pnas.2119695119
    tissue_or_cell_type
    Purified wild-type G6PD and D200N

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 762–773

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

    ### glutathione-g6pd-nadph Human G6PD uses glucose-6-phosphate and catalytic NADP+ to generate NADPH. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The reducing power used in glutathione recycling has to be replenished. organism: Human tissue_or_cell_type: Purified wild-type G6PD and D200N experimental_model: Cryo-EM and structural comparison limitations: Structural NADP and catalytic NADP are different sites; enzyme activity is not a niacin-treatment trial. exposure: Ligand-free and NADP/G6P-bound states evidence_span: {"source_cache": "artifacts/glutathione-research/35858355.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "02c2d0e880b17ab304fab0854064813ffec5fa9e647b978a083aa88fbf8a38f0", "start_char": 0, "end_char": 1328, "text_sha256": "02c2d0e880b17ab304fab0854064813ffec5fa9e647b978a083aa88fbf8a38f0"} [glutathione-p35858355] Allosteric role of a structural NADP+ molecule in glucose-6-phosphate dehydrogenase activity. (2022). https://pubmed.ncbi.nlm.nih.gov/35858355/ DOI: 10.1073/pnas.2119695119
    Complete structured claim and evidence

What acts on it

  1. Sulforaphane increased G6PD expression in the fibroblast study.

    Sulforaphane / SFN, stereochemistry specified per study → Glucose-6-phosphate dehydrogenase / G6PD source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"}
    experimental_model
    Replicative culture and metabolic/gene-expression measurements
    exposure
    Sulforaphane treatment during serial culture
    limitations
    Cell-culture senescence is not human longevity; expression is not necessarily flux.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Human MRC-5 and BJ fibroblasts
    plain_language
    The response includes machinery connected to the cellular reducing-power supply.
    primary_references
    [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
    tissue_or_cell_type
    Glucose handling, antioxidant response and senescence

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 879–890

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Replicative culture and metabolic/gene-expression measurements · source_derived_draft · unverified_draft

    ### sulforaphane-g6pd-expression Sulforaphane increased G6PD expression in the fibroblast study. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The response includes machinery connected to the cellular reducing-power supply. organism: Human MRC-5 and BJ fibroblasts tissue_or_cell_type: Glucose handling, antioxidant response and senescence experimental_model: Replicative culture and metabolic/gene-expression measurements limitations: Cell-culture senescence is not human longevity; expression is not necessarily flux. exposure: Sulforaphane treatment during serial culture evidence_span: {"source_cache": "artifacts/sulforaphane-research/30595796.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274", "start_char": 0, "end_char": 2097, "text_sha256": "aa7d5e0ef15224906eb42eb49309439c966c30310740dbdea9553b76b2f91274"} [sulforaphane-p30595796] Sulforaphane Delays Fibroblast Senescence by Curbing Cellular Glucose Uptake, Increased Glycolysis, and Oxidative Damage. (2018). https://pubmed.ncbi.nlm.nih.gov/30595796/ DOI: 10.1155/2018/5642148
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Low FMN-dependent PNP oxidase activity in many G6PD-deficient participants responded to oral riboflavin despite the contrasting FAD-saturated GSR pattern.

    Riboflavin (vitamin B2) → Erythrocyte pyridoxamine/pyridoxine phosphate oxidase activity source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    cross_nutrient
    B2 cofactor supply affects a B6-activation assay.
    experimental_model
    Human erythrocytes from G6PD deficiency, heterozygous beta-thalassemia and controls.
    exposure
    In-vitro FAD stimulation of glutathione reductase and PNP oxidase activity, with oral-riboflavin response observations.
    limitations
    No isolated whole-body B6 flux or clinical seizure/neuropathy outcome was established.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Homo sapiens
    plain_language
    FMN and FAD should not be treated as one interchangeable vitamin pool.
    primary_references
    [b2-anderson1987] Glutathione reductase activity and its relationship to pyridoxine phosphate activity in G6PD deficiency (1987). https://pubmed.ncbi.nlm.nih.gov/3582603/ DOI: 10.1111/j.1600-0609.1987.tb01417.x
    tissue_or_cell_type
    Human clinical setting
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1679–1690

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human erythrocytes from G6PD deficiency, heterozygous beta-thalassemia and controls. · source_derived_draft · unverified_draft

    ### b2-g6pd-fmn-oxidase-response Low FMN-dependent PNP oxidase activity in many G6PD-deficient participants responded to oral riboflavin despite the contrasting FAD-saturated GSR pattern. Condition category: biomarker_context nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: FMN and FAD should not be treated as one interchangeable vitamin pool. organism: Homo sapiens tissue_or_cell_type: Human clinical setting experimental_model: Human erythrocytes from G6PD deficiency, heterozygous beta-thalassemia and controls. limitations: No isolated whole-body B6 flux or clinical seizure/neuropathy outcome was established. exposure: In-vitro FAD stimulation of glutathione reductase and PNP oxidase activity, with oral-riboflavin response observations. cross_nutrient: B2 cofactor supply affects a B6-activation assay. [b2-anderson1987] Glutathione reductase activity and its relationship to pyridoxine phosphate activity in G6PD deficiency (1987). https://pubmed.ncbi.nlm.nih.gov/3582603/ DOI: 10.1111/j.1600-0609.1987.tb01417.x
    Complete structured claim and evidence

  2. Human erythrocytes reduced lipoic acid to DHLA with glucose but not with 2-deoxyglucose, supporting NADPH dependence.

    Lipoic acid → Erythrocyte reduction of free lipoic acid source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/ala-research/7632170.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707", "start_char": 0, "end_char": 1863, "text_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707"}
    experimental_model
    Human erythrocytes, one G6PD-deficient donor and purified-enzyme assays
    exposure
    Lipoic acid with glucose/2-deoxyglucose and G6PD inhibition
    limitations
    The deficient-donor finding is small and mechanistic; it is not a clinical safety or efficacy trial in G6PD deficiency.
    nutrient_topic
    Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. · Lipoic acid
    organism
    Human
    plain_language
    The cell must supply reducing power to make DHLA.
    primary_references
    [ala-p7632170] Reduction and transport of lipoic acid by human erythrocytes. (1995). https://pubmed.ncbi.nlm.nih.gov/7632170/ DOI: 10.1016/0006-2952(95)00084-d
    tissue_or_cell_type
    Erythrocytes and glutathione reductase

    Alpha-lipoic acid: cofactor assembly, redox signaling and nutrient interactions (2026-09-17) · lines 715–726

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human erythrocytes, one G6PD-deficient donor and purified-enzyme assays · source_derived_draft · unverified_draft

    ### ala-rbc-glucose-reduction Human erythrocytes reduced lipoic acid to DHLA with glucose but not with 2-deoxyglucose, supporting NADPH dependence. Condition category: normal nutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: The cell must supply reducing power to make DHLA. organism: Human tissue_or_cell_type: Erythrocytes and glutathione reductase experimental_model: Human erythrocytes, one G6PD-deficient donor and purified-enzyme assays limitations: The deficient-donor finding is small and mechanistic; it is not a clinical safety or efficacy trial in G6PD deficiency. exposure: Lipoic acid with glucose/2-deoxyglucose and G6PD inhibition evidence_span: {"source_cache": "artifacts/ala-research/7632170.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707", "start_char": 0, "end_char": 1863, "text_sha256": "2ebbc851e5279e646bc7c892645c931a3fd2993830c3f4405379839cbbd6e707"} [ala-p7632170] Reduction and transport of lipoic acid by human erythrocytes. (1995). https://pubmed.ncbi.nlm.nih.gov/7632170/ DOI: 10.1016/0006-2952(95)00084-d
    Complete structured claim and evidence

  3. Structural-site NADP+ binding ordered the G6PD C-terminal region and supported substrate binding and catalysis.

    NADP+ → Human G6PD glucose-6-phosphate binding and catalysis source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/35858355.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "02c2d0e880b17ab304fab0854064813ffec5fa9e647b978a083aa88fbf8a38f0", "start_char": 0, "end_char": 1328, "text_sha256": "02c2d0e880b17ab304fab0854064813ffec5fa9e647b978a083aa88fbf8a38f0"}
    experimental_model
    Cryo-EM and structural comparison
    exposure
    Ligand-free and NADP/G6P-bound states
    limitations
    Structural NADP and catalytic NADP are different sites; enzyme activity is not a niacin-treatment trial.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human
    plain_language
    The same coenzyme also has a distinct structural regulatory role.
    primary_references
    [glutathione-p35858355] Allosteric role of a structural NADP+ molecule in glucose-6-phosphate dehydrogenase activity. (2022). https://pubmed.ncbi.nlm.nih.gov/35858355/ DOI: 10.1073/pnas.2119695119
    tissue_or_cell_type
    Purified wild-type G6PD and D200N

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 775–786

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

    ### glutathione-g6pd-structural-nadp Structural-site NADP+ binding ordered the G6PD C-terminal region and supported substrate binding and catalysis. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same coenzyme also has a distinct structural regulatory role. organism: Human tissue_or_cell_type: Purified wild-type G6PD and D200N experimental_model: Cryo-EM and structural comparison limitations: Structural NADP and catalytic NADP are different sites; enzyme activity is not a niacin-treatment trial. exposure: Ligand-free and NADP/G6P-bound states evidence_span: {"source_cache": "artifacts/glutathione-research/35858355.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "02c2d0e880b17ab304fab0854064813ffec5fa9e647b978a083aa88fbf8a38f0", "start_char": 0, "end_char": 1328, "text_sha256": "02c2d0e880b17ab304fab0854064813ffec5fa9e647b978a083aa88fbf8a38f0"} [glutathione-p35858355] Allosteric role of a structural NADP+ molecule in glucose-6-phosphate dehydrogenase activity. (2022). https://pubmed.ncbi.nlm.nih.gov/35858355/ DOI: 10.1073/pnas.2119695119
    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