Component

Staphylococcus aureus bacillithiol-disulfide reductase / YpdA

Staphylococcus aureus bacillithiol-disulfide reductase / YpdA. 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. YpdA accepted the allyl-bacillithiol adduct BSSA as a substrate to regenerate bacillithiol.

    Staphylococcus aureus bacillithiol-disulfide reductase / YpdA → Bacillithiol / BSH Recorded from sourceungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.
    experimental_model
    Purified bacterial reductase assay; abstract-level access.
    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
    YpdA accepted the allyl-bacillithiol adduct BSSA as a substrate to regenerate bacillithiol.
    primary_references
    Staphylococcus aureus responds to allicin by global S-thioallylation - Role of the Brx/BSH/YpdA pathway and the disulfide reductase MerA to overcome allicin stress. | 2019 | DOI 10.1016/j.freeradbiomed.2019.05.018 | PMID 31121222 | https://pubmed.ncbi.nlm.nih.gov/31121222/ | https://doi.org/10.1016/j.freeradbiomed.2019.05.018
    source_locator
    Reviewed reference lines 51-51; exact primary location described in quoted passage where extracted.

    Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 51–51

    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 bacterial reductase assay; abstract-level access. · Recorded from source · Recorded from source

    **Bacterial thiol systems differ.** Staphylococcus aureus uses bacillithiol rather than treating glutathione as its universal buffer. The 2019 study reported a bacillithiol redox shift, protein S-thioallylation, and reversal through bacilliredoxin/bacillithiol/YpdA chemistry; YpdA could use the allyl-bacillithiol adduct to regenerate bacillithiol. These are organism-specific repair findings, not evidence for the same proteins in humans. [Loi 2019](https://pubmed.ncbi.nlm.nih.gov/31121222/)
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. The bacilliredoxin/bacillithiol/YpdA pathway reversed protein S-thioallylation in the reported biochemical study.

    Staphylococcus aureus bacilliredoxin/bacillithiol/YpdA repair system → Protein S-thioallylation in Staphylococcus aureus Recorded from sourceungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.
    experimental_model
    Staphylococcus aureus biochemical repair evidence; abstract-level access.
    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
    The bacilliredoxin/bacillithiol/YpdA pathway reversed protein S-thioallylation in the reported biochemical study.
    primary_references
    Staphylococcus aureus responds to allicin by global S-thioallylation - Role of the Brx/BSH/YpdA pathway and the disulfide reductase MerA to overcome allicin stress. | 2019 | DOI 10.1016/j.freeradbiomed.2019.05.018 | PMID 31121222 | https://pubmed.ncbi.nlm.nih.gov/31121222/ | https://doi.org/10.1016/j.freeradbiomed.2019.05.018
    source_locator
    Reviewed reference lines 51-51; exact primary location described in quoted passage where extracted.

    Allicin: detailed mechanisms of action (reviewed 5 October 2026) · lines 51–51

    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 · Staphylococcus aureus biochemical repair evidence; abstract-level access. · Recorded from source · Recorded from source

    **Bacterial thiol systems differ.** Staphylococcus aureus uses bacillithiol rather than treating glutathione as its universal buffer. The 2019 study reported a bacillithiol redox shift, protein S-thioallylation, and reversal through bacilliredoxin/bacillithiol/YpdA chemistry; YpdA could use the allyl-bacillithiol adduct to regenerate bacillithiol. These are organism-specific repair findings, not evidence for the same proteins in humans. [Loi 2019](https://pubmed.ncbi.nlm.nih.gov/31121222/)
    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.