Component

Glutathione peroxidase with glutathione as a peroxide-removing system

Glutathione peroxidase with glutathione as a peroxide-removing system. Species, exposure and limitations are retained in each linked claim.

1 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.

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)

  1. The potency of acetaminophen against both purified ovine cyclooxygenase-1 and human cyclooxygenase-2 was increased approximately 30-fold by the presence of glutathione peroxidase and glutathione, giving half-maximal inhibitory concentrations of 33 and 980 micromolar respectively, acetaminophen was found to be a good reducing agent of both enzymes, and the results are consistent with a mechanism in which it reduces the active oxidized form of the enzyme to the resting form, so that inhibition would be more effective under conditions of low peroxide concentration, consistent with the known tissue selectivity.

    Paracetamol → Cyclooxygenase-1 (PTGS1) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/paracetamol-research/11370851.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4eeda4b163828f2cc2a4341c4810df6bf6c683d6165eeb09479104f185e52ca4", "start_char": 0, "end_char": 1086, "text_sha256": "4eeda4b163828f2cc2a4341c4810df6bf6c683d6165eeb09479104f185e52ca4"}
    experimental_model
    Purified ovine cyclooxygenase-1 and human cyclooxygenase-2 assayed with and without a peroxide-removing system
    exposure
    Acetaminophen with and without glutathione peroxidase and glutathione
    limitations
    Adding a peroxide-removing system is the manipulation that reveals the mechanism, because it changes potency thirtyfold without changing the drug. Purified enzyme, so the concentrations are not tissue concentrations.
    nutrient_topic
    Paracetamol research collection; topical membership is not evidence of a direct clinical effect, and the drug is recorded separately from the metabolites NAPQI and AM404. · Paracetamol
    organism
    Sheep and human enzyme
    plain_language
    Take the peroxide away and the same drug becomes thirty times stronger, which is the whole mechanism in one experiment.
    primary_references
    [apap-p11370851] Mechanism of acetaminophen inhibition of cyclooxygenase isoforms. (2001). https://pubmed.ncbi.nlm.nih.gov/11370851/ DOI: 10.1006/abbi.2000.2232
    tissue_or_cell_type
    Purified cyclooxygenase

    Paracetamol: the enzyme it reduces rather than blocks, the isoform that turned out not to exist, the metabolite that carries the analgesia, and the metabolite that destroys the liver (2026-09-22) · lines 77–88

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified ovine cyclooxygenase-1 and human cyclooxygenase-2 assayed with and without a peroxide-removing system · source_derived_draft · unverified_draft

    ### apap-potency-depends-on-peroxide The potency of acetaminophen against both purified ovine cyclooxygenase-1 and human cyclooxygenase-2 was increased approximately 30-fold by the presence of glutathione peroxidase and glutathione, giving half-maximal inhibitory concentrations of 33 and 980 micromolar respectively, acetaminophen was found to be a good reducing agent of both enzymes, and the results are consistent with a mechanism in which it reduces the active oxidized form of the enzyme to the resting form, so that inhibition would be more effective under conditions of low peroxide concentration, consistent with the known tissue selectivity. Condition category: normal nutrient_topic: Paracetamol research collection; topical membership is not evidence of a direct clinical effect, and the drug is recorded separately from the metabolites NAPQI and AM404. plain_language: Take the peroxide away and the same drug becomes thirty times stronger, which is the whole mechanism in one experiment. organism: Sheep and human enzyme tissue_or_cell_type: Purified cyclooxygenase experimental_model: Purified ovine cyclooxygenase-1 and human cyclooxygenase-2 assayed with and without a peroxide-removing system limitations: Adding a peroxide-removing system is the manipulation that reveals the mechanism, because it changes potency thirtyfold without changing the drug. Purified enzyme, so the concentrations are not tissue concentrations. exposure: Acetaminophen with and without glutathione peroxidase and glutathione evidence_span: {"source_cache": "artifacts/paracetamol-research/11370851.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4eeda4b163828f2cc2a4341c4810df6bf6c683d6165eeb09479104f185e52ca4", "start_char": 0, "end_char": 1086, "text_sha256": "4eeda4b163828f2cc2a4341c4810df6bf6c683d6165eeb09479104f185e52ca4"} [apap-p11370851] Mechanism of acetaminophen inhibition of cyclooxygenase isoforms. (2001). https://pubmed.ncbi.nlm.nih.gov/11370851/ DOI: 10.1006/abbi.2000.2232
    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.

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