Component

Saccharomyces cerevisiae glutathione reductase / Glr1

Saccharomyces cerevisiae glutathione reductase / Glr1. Interpret through the linked study species, preparation, exposure and measured endpoint.

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 it acts on

  1. Purified yeast glutathione reductase used GSSA as a substrate with NADPH consumption; apparent Km was 0.50 mM.

    Saccharomyces cerevisiae glutathione reductase / Glr1 → NADPH-dependent GSSA reduction by purified yeast glutathione reductase source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text available; selected claim-relevant methods, results, tables/figures and limitations reviewed. Supplemental proteome and all secondary findings are not exhaustively extracted.
    experimental_model
    Purified commercial Saccharomyces cerevisiae enzyme; NADPH absorbance assay without DTNB.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Not human GSR validation. GSSG comparator used a different assay, and Km alone does not measure catalytic efficiency.
    plain_language
    Purified yeast glutathione reductase used GSSA as a substrate with NADPH consumption; apparent Km was 0.50 mM.
    primary_references
    <i>S</i>-allylmercaptoglutathione Is a Substrate for Glutathione Reductase (E.C. 1.8.1.7) from Yeast (<i>Saccharomyces cerevisiae</i>). | 2018 | DOI 10.3390/antiox7070086 | PMID 29986384 | https://pubmed.ncbi.nlm.nih.gov/29986384/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC6070820/ | https://doi.org/10.3390/antiox7070086
    source_locator
    Reviewed reference lines 47-47; exact primary location described in quoted passage where extracted.

    Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 47–47

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Purified commercial Saccharomyces cerevisiae enzyme; NADPH absorbance assay without DTNB. · source_derived_draft · unverified_draft

    **GSSA recycling and NADPH.** Purified yeast glutathione reductase reduced GSSA with NADPH consumption. Reported apparent Km values were 0.50 mM for GSSA and 0.07 mM for GSSG. They do not establish an eightfold difference in catalytic efficiency: turnover and assay differences matter, and the GSSA measurement deliberately omitted the DTNB cycling reagent used for GSSG. GSSA also supported growth of glutathione-synthesis-defective yeast. That rescue is consistent with recovery of usable glutathione, but it is not a human GSR experiment or proof that this enzyme was the exclusive route in living cells. [Horn 2018](https://pmc.ncbi.nlm.nih.gov/articles/PMC6070820/)
    Complete structured claim and evidence

  2. Loss of yeast-glr1 increased susceptibility in the allicin arm of the yeast chemical-genetic comparison.

    Saccharomyces cerevisiae glutathione reductase / Glr1 → Saccharomyces cerevisiae growth during allicin exposure source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text available; selected claim-relevant methods, results, tables/figures and limitations reviewed. Supplemental proteome and all secondary findings are not exhaustively extracted.
    experimental_condition
    Wild-type yeast at the same allicin exposure deleted · Saccharomyces cerevisiae glutathione reductase / Glr1 Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_condition
    Wild-type yeast at the same allicin exposure present · Allicin Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_contrast
    {"intervention": "yeast-glr1 deletion with allicin", "comparator": "Wild-type yeast at the same allicin exposure", "endpoint": "Loss of yeast-glr1 increased susceptibility in the allicin arm of the yeast chemical-genetic comparison.", "effect_direction": "decrease", "combination": "joint", "conditions": [{"entity_slug": "yeast-glr1", "state": "deleted"}, {"entity_slug": "allicin", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Saccharomyces cerevisiae; separate gene deletions and allicin exposures compared with an analogue; Figure 3.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Keep dose and compound distinctions: analogue effects cannot substitute for allicin. Not a human nutrient-deficiency phenotype.
    plain_language
    Loss of yeast-glr1 increased susceptibility in the allicin arm of the yeast chemical-genetic comparison.
    primary_references
    The Sulfilimine Analogue of Allicin, <i>S</i>-Allyl-<i>S</i>-(<i>S</i>-allyl)-<i>N</i>-Cyanosulfilimine, Is Antimicrobial and Reacts with Glutathione. | 2020 | DOI 10.3390/antiox9111086 | PMID 33158268 | https://pubmed.ncbi.nlm.nih.gov/33158268/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7694261/ | https://doi.org/10.3390/antiox9111086
    source_locator
    Reviewed reference lines 49-49; exact primary location described in quoted passage where extracted.
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 49–49

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Saccharomyces cerevisiae; separate gene deletions and allicin exposures compared with an analogue; Figure 3. · source_derived_draft · unverified_draft

    **Redox-defense impairment.** A study comparing allicin with a sulfilimine analogue included allicin-exposed Saccharomyces cerevisiae mutants. The GLR1, ZWF1, and YAP1 perturbations connect susceptibility to glutathione recycling, NADPH supply, and stress regulation; effects depended on concentration and compound. The analogue was more potent in some low-concentration comparisons, and its results must not be copied onto allicin. TRX2 loss had a much smaller effect in this system. Human B2 deficiency, G6PD deficiency, or selenium status cannot be assigned the yeast phenotype without direct evidence. [Horn 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7694261/)
    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.