Component

Purified human GAPDH catalytic activity

Purified human GAPDH catalytic activity. Species, exposure and limitations are retained in each linked claim.

2 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 acts on it

  1. GAPDH S-glutathionylation did not itself inactivate the enzyme in this assay.

    S-Glutathionylation of purified human GAPDH → Purified human GAPDH catalytic activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/9642155.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72", "start_char": 0, "end_char": 1538, "text_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72"}
    experimental_model
    Purified GAPDH oxidation and radiolabeled disulfide assays
    exposure
    Hydrogen peroxide versus GSSG and glutaredoxin
    limitations
    This particular assay separates oxidation from glutathionylation; it does not establish one universal effect for all modified proteins.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human GAPDH; human or bacterial glutaredoxin
    plain_language
    A glutathione tag is not automatically a protein-off switch.
    primary_references
    [glutathione-p9642155] Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. (1998). https://pubmed.ncbi.nlm.nih.gov/9642155/ DOI: 10.1006/bbrc.1998.8695
    tissue_or_cell_type
    Cell-free enzyme system

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 840–851

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified GAPDH oxidation and radiolabeled disulfide assays · source_derived_draft · unverified_draft

    ### glutathione-gapdh-glutathionylation-null GAPDH S-glutathionylation did not itself inactivate the enzyme in this assay. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: A glutathione tag is not automatically a protein-off switch. organism: Human GAPDH; human or bacterial glutaredoxin tissue_or_cell_type: Cell-free enzyme system experimental_model: Purified GAPDH oxidation and radiolabeled disulfide assays limitations: This particular assay separates oxidation from glutathionylation; it does not establish one universal effect for all modified proteins. exposure: Hydrogen peroxide versus GSSG and glutaredoxin evidence_span: {"source_cache": "artifacts/glutathione-research/9642155.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72", "start_char": 0, "end_char": 1538, "text_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72"} [glutathione-p9642155] Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. (1998). https://pubmed.ncbi.nlm.nih.gov/9642155/ DOI: 10.1006/bbrc.1998.8695
    Complete structured claim and evidence

  2. Direct hydrogen-peroxide oxidation inhibited GAPDH activity in the comparison.

    Hydrogen peroxide → Purified human GAPDH catalytic activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/9642155.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72", "start_char": 0, "end_char": 1538, "text_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72"}
    experimental_model
    Purified GAPDH oxidation and radiolabeled disulfide assays
    exposure
    Hydrogen peroxide versus GSSG and glutaredoxin
    limitations
    This particular assay separates oxidation from glutathionylation; it does not establish one universal effect for all modified proteins.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human GAPDH; human or bacterial glutaredoxin
    plain_language
    The kind of chemical modification mattered.
    primary_references
    [glutathione-p9642155] Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. (1998). https://pubmed.ncbi.nlm.nih.gov/9642155/ DOI: 10.1006/bbrc.1998.8695
    tissue_or_cell_type
    Cell-free enzyme system

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 853–864

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified GAPDH oxidation and radiolabeled disulfide assays · source_derived_draft · unverified_draft

    ### glutathione-gapdh-peroxide Direct hydrogen-peroxide oxidation inhibited GAPDH activity in the comparison. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The kind of chemical modification mattered. organism: Human GAPDH; human or bacterial glutaredoxin tissue_or_cell_type: Cell-free enzyme system experimental_model: Purified GAPDH oxidation and radiolabeled disulfide assays limitations: This particular assay separates oxidation from glutathionylation; it does not establish one universal effect for all modified proteins. exposure: Hydrogen peroxide versus GSSG and glutaredoxin evidence_span: {"source_cache": "artifacts/glutathione-research/9642155.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72", "start_char": 0, "end_char": 1538, "text_sha256": "701b6cbdc44486c0b9423d7c30f52b282f1407958c7dde45d4aa1d3751718a72"} [glutathione-p9642155] Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. (1998). https://pubmed.ncbi.nlm.nih.gov/9642155/ DOI: 10.1006/bbrc.1998.8695
    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