Component

S-Allylmercaptoglutathione / GSSA

S-Allylmercaptoglutathione / GSSA. Interpret through the linked study species, preparation, exposure and measured endpoint.

3 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. GSSA supplementation supported growth of GSH1-deficient yeast on otherwise glutathione-unsupplemented medium.

    S-Allylmercaptoglutathione / GSSA → Growth of yeast lacking GSH1 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
    GSH1-deficient yeast without exogenous glutathione source deleted · Saccharomyces cerevisiae glutamate-cysteine ligase Gsh1 Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_condition
    GSH1-deficient yeast without exogenous glutathione source supplied · S-Allylmercaptoglutathione / GSSA Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_contrast
    {"intervention": "GSSA supplied to GSH1-deficient yeast", "comparator": "GSH1-deficient yeast without exogenous glutathione source", "endpoint": "GSSA supplementation supported growth of GSH1-deficient yeast on otherwise glutathione-unsupplemented medium.", "effect_direction": "increase", "combination": "joint", "conditions": [{"entity_slug": "yeast-gsh1", "state": "deleted"}, {"entity_slug": "s-allylmercaptoglutathione", "state": "supplied"}]} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Saccharomyces cerevisiae GSH1 deletion; GSSA compared with unsupplemented growth medium.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Rescue supports usable GSH recovery but does not prove the exclusive in vivo reductase or human rescue.
    plain_language
    GSSA supplementation supported growth of GSH1-deficient yeast on otherwise glutathione-unsupplemented medium.
    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.
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    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 · Saccharomyces cerevisiae GSH1 deletion; GSSA compared with unsupplemented growth medium. · 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

What acts on it

  1. Allicin reacts with glutathione to form GSSA, distinct from GSSG.

    Allicin → S-Allylmercaptoglutathione / GSSA 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
    Cell-free product preparation and LC-MS characterization; not human oral metabolism.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.
    plain_language
    Allicin reacts with glutathione to form GSSA, distinct from GSSG.
    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 39-39; exact primary location described in quoted passage where extracted.

    Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 39–39

    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 · Cell-free product preparation and LC-MS characterization; not human oral metabolism. · source_derived_draft · unverified_draft

    **Thioallylation chemistry.** Allicin reacts with accessible cysteine thiols to form allyl-containing mixed disulfides. For a protein, the simplified first reaction is protein-SH + allicin → protein-S-S-allyl + allylsulfenic acid. Glutathione forms S-allylmercaptoglutathione (GSSA), which is chemically distinct from oxidized glutathione (GSSG). Accessibility, local environment, competing thiols, and exposure determine which targets are modified. An adduct alone does not demonstrate inhibition, phenotype mediation, or dietary target engagement. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/) [Horn 2018](https://pmc.ncbi.nlm.nih.gov/articles/PMC6070820/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  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

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.