Component

Human MPST mitochondrial isoform 2

A splice isoform of the existing human MPST protein; not a new gene or a mouse ortholog. The cited target-binding experiment uses this recombinant construct.

4 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. Human MPST2 is a mitochondrial-targeted splice isoform of MPST, distinct from cytosolic MPST1.

    Human MPST mitochondrial isoform 2 → Human mercaptopyruvate sulfurtransferase / MPST source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary indexed abstract and figure descriptions.
    experimental_model
    Recombinant human isoform characterization and sequence organisation.
    interpretation_status
    Source-derived research curation; not independent raw-data verification.
    limitations
    An isoform relationship is identity/navigation, not a signed activation effect; it does not collapse mouse and human proteins.
    nutrient_topic
    Ergothioneine mitochondrial supplement; shared molecular requirements are not demonstrated dietary interactions. · L-Ergothioneine
    plain_language
    This is the same human enzyme family with a specific splice form.
    primary_references
    Yadav et al. Thioredoxin regulates human mercaptopyruvate sulfurtransferase at physiologically-relevant concentrations. DOI 10.1074/jbc.RA120.012616; PMID 32179647; https://pubmed.ncbi.nlm.nih.gov/32179647/
    source_locator
    Abstract and Figure 1

    Ergothioneine: mitochondrial transport, MPST and sulfur-handling dependencies (2026-10-02) · lines 41–41

    Original AI-assisted curation of five primary studies with publication identifiers, experimental locators and access limitations. Additive chapter supplement, not publisher full text. · supports · Recombinant human isoform characterization and sequence organisation. · source_derived_draft · unverified_draft

    Human MPST2 is a mitochondrial-targeted splice isoform of MPST, distinct from cytosolic MPST1.
    Complete structured claim and evidence

What acts on it

  1. Ergothioneine bound purified human MPST2 in ITC and NMR experiments.

    L-Ergothioneine → Human MPST mitochondrial isoform 2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Publisher abstract/introduction plus the authors' article and supplementary legends reproduced in an indexed document. This is source-derived extraction, not raw-data verification. Main-text OCR corrupts some micro-unit symbols; ambiguous doses and binding constants are deliberately not transcribed.
    experimental_model
    Purified recombinant human MPST mitochondrial isoform 2.
    interpretation_status
    Source-derived research curation; not independent raw-data verification.
    limitations
    Binding is measured; docking poses and proposed sulfur-acceptor chemistry are not equivalent to a measured covalent intermediate. Ambiguous OCR binding constants are omitted.
    nutrient_topic
    Ergothioneine mitochondrial supplement; shared molecular requirements are not demonstrated dietary interactions. · L-Ergothioneine
    organism
    Homo sapiens
    plain_language
    Ergothioneine has an experimentally identified enzyme target.
    primary_references
    Sprenger et al. Ergothioneine controls mitochondrial function and exercise performance via direct activation of MPST. DOI 10.1016/j.cmet.2025.01.024; PMID 39965563; https://pubmed.ncbi.nlm.nih.gov/39965563/
    protein_isoform
    MPST2 · Human MPST mitochondrial isoform 2
    source_locator
    Figure 3E; Figures S3E-S3G; Results

    Ergothioneine: mitochondrial transport, MPST and sulfur-handling dependencies (2026-10-02) · lines 49–49

    Original AI-assisted curation of five primary studies with publication identifiers, experimental locators and access limitations. Additive chapter supplement, not publisher full text. · supports · Purified recombinant human MPST mitochondrial isoform 2. · source_derived_draft · unverified_draft

    Ergothioneine bound purified human MPST2 in ITC and NMR experiments.
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Without 3-mercaptopyruvate, ergothioneine produced no detected H2S in the MPST and isolated-mitochondria assays.

    L-Ergothioneine → Hydrogen sulfide / H2S source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Publisher abstract/introduction plus the authors' article and supplementary legends reproduced in an indexed document. This is source-derived extraction, not raw-data verification. Main-text OCR corrupts some micro-unit symbols; ambiguous doses and binding constants are deliberately not transcribed.
    experimental_condition
    substrate-omission baseline controls present · L-Ergothioneine Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_condition
    substrate-omission baseline controls omitted · 3-Mercaptopyruvate Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_contrast
    {"intervention": "ergothioneine with 3-mercaptopyruvate omitted", "comparator": "substrate-omission baseline controls", "endpoint": "detectable H2S signal", "effect_direction": "no_detected_change", "combination": "joint", "conditions": [{"entity_slug": "ergothioneine", "state": "present"}, {"entity_slug": "3-mercaptopyruvate", "state": "omitted"}]} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Recombinant MPST and isolated mitochondria; substrate-omission controls.
    interpretation_status
    Source-derived research curation; not independent raw-data verification.
    limitations
    This control is not evidence of a human 3-mercaptopyruvate deficiency threshold or a universal inability to release sulfur in other systems.
    nutrient_topic
    Ergothioneine mitochondrial supplement; shared molecular requirements are not demonstrated dietary interactions. · L-Ergothioneine
    plain_language
    Ergothioneine alone did not replace the substrate.
    primary_references
    Sprenger et al. Ergothioneine controls mitochondrial function and exercise performance via direct activation of MPST. DOI 10.1016/j.cmet.2025.01.024; PMID 39965563; https://pubmed.ncbi.nlm.nih.gov/39965563/
    source_locator
    Figures S3K-S3L; Results

    Ergothioneine: mitochondrial transport, MPST and sulfur-handling dependencies (2026-10-02) · lines 65–65

    Original AI-assisted curation of five primary studies with publication identifiers, experimental locators and access limitations. Additive chapter supplement, not publisher full text. · supports · Recombinant MPST and isolated mitochondria; substrate-omission controls. · source_derived_draft · unverified_draft

    Without 3-mercaptopyruvate, ergothioneine produced no detected H2S in the MPST and isolated-mitochondria assays.
    Complete structured claim and evidence

  2. Ergothioneine plus 3-mercaptopyruvate supported H2S release by recombinant human MPST.

    L-Ergothioneine → Hydrogen sulfide / H2S source_derived_draftungraded
    Experimental context and source evidence
    assay_pH
    11
    evidence_access
    Publisher abstract/introduction plus the authors' article and supplementary legends reproduced in an indexed document. This is source-derived extraction, not raw-data verification. Main-text OCR corrupts some micro-unit symbols; ambiguous doses and binding constants are deliberately not transcribed.
    experimental_condition
    substrate conditions without ergothioneine added · L-Ergothioneine Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_condition
    substrate conditions without ergothioneine present · 3-Mercaptopyruvate Condition belongs to the full experimental contrast; do not separate a joint intervention.
    experimental_contrast
    {"intervention": "ergothioneine plus 3-mercaptopyruvate", "comparator": "substrate conditions without ergothioneine", "endpoint": "AzMC H2S-associated signal", "effect_direction": "increase", "combination": "joint", "conditions": [{"entity_slug": "ergothioneine", "state": "added"}, {"entity_slug": "3-mercaptopyruvate", "state": "present"}]} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Purified human MPST activity assay using AzMC; reported buffer pH 11.
    interpretation_status
    Source-derived research curation; not independent raw-data verification.
    limitations
    The alkaline biochemical assay does not establish the same flux at physiological pH. Product signal is not proof of a structurally identified ergothioneine persulfide.
    nutrient_topic
    Ergothioneine mitochondrial supplement; shared molecular requirements are not demonstrated dietary interactions. · L-Ergothioneine
    plain_language
    Enzyme activation still needs its sulfur substrate.
    primary_references
    Sprenger et al. Ergothioneine controls mitochondrial function and exercise performance via direct activation of MPST. DOI 10.1016/j.cmet.2025.01.024; PMID 39965563; https://pubmed.ncbi.nlm.nih.gov/39965563/
    source_locator
    Figure 3G; Figure S3K; STAR Methods, Recombinant MPST activity

    Ergothioneine: mitochondrial transport, MPST and sulfur-handling dependencies (2026-10-02) · lines 57–57

    Original AI-assisted curation of five primary studies with publication identifiers, experimental locators and access limitations. Additive chapter supplement, not publisher full text. · supports · Purified human MPST activity assay using AzMC; reported buffer pH 11. · source_derived_draft · unverified_draft

    Ergothioneine plus 3-mercaptopyruvate supported H2S release by recombinant human MPST.
    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