Component

Human glutaredoxin 2 / GLRX2

Human glutaredoxin 2 / GLRX2. Species, exposure and limitations are retained in each linked claim.

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. GLRX2 reduced glutathionylated substrates with lower rate but higher affinity than GLRX1, giving similar catalytic efficiency.

    Human glutaredoxin 2 / GLRX2 → Human GLRX2-mediated protein deglutathionylation source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/14676218.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84", "start_char": 0, "end_char": 1398, "text_sha256": "a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84"}
    experimental_model
    Purified human glutaredoxin kinetics and mutants
    exposure
    GSH or NADPH/thioredoxin-reductase donor systems
    limitations
    Biochemical electron-donor alternatives; no claim that all cellular GLRX2 uses one route.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human GLRX1/GLRX2
    plain_language
    Glutathione attached to a protein can be removed enzymatically.
    primary_references
    [glutathione-p14676218] Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. (2004). https://pubmed.ncbi.nlm.nih.gov/14676218/ DOI: 10.1074/jbc.m312719200
    tissue_or_cell_type
    Glutathionylated substrates

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 814–825

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human glutaredoxin kinetics and mutants · source_derived_draft · unverified_draft

    ### glutathione-glrx2-deglutathionylation GLRX2 reduced glutathionylated substrates with lower rate but higher affinity than GLRX1, giving similar catalytic efficiency. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutathione attached to a protein can be removed enzymatically. organism: Human GLRX1/GLRX2 tissue_or_cell_type: Glutathionylated substrates experimental_model: Purified human glutaredoxin kinetics and mutants limitations: Biochemical electron-donor alternatives; no claim that all cellular GLRX2 uses one route. exposure: GSH or NADPH/thioredoxin-reductase donor systems evidence_span: {"source_cache": "artifacts/glutathione-research/14676218.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84", "start_char": 0, "end_char": 1398, "text_sha256": "a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84"} [glutathione-p14676218] Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. (2004). https://pubmed.ncbi.nlm.nih.gov/14676218/ DOI: 10.1074/jbc.m312719200
    Complete structured claim and evidence

What acts on it

  1. A thioredoxin-reductase/NADPH system reduced GLRX2 disulfide and GSH-GLRX2 intermediates.

    NADPH → Human glutaredoxin 2 / GLRX2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/14676218.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84", "start_char": 0, "end_char": 1398, "text_sha256": "a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84"}
    experimental_model
    Purified human glutaredoxin kinetics and mutants
    exposure
    GSH or NADPH/thioredoxin-reductase donor systems
    limitations
    Thioredoxin-reductase isoform is not assigned from the indexed abstract; this is not a new selenium-dose response.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human GLRX1/GLRX2
    plain_language
    Glutaredoxin recovery also had an alternative donor route in the assay.
    primary_references
    [glutathione-p14676218] Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. (2004). https://pubmed.ncbi.nlm.nih.gov/14676218/ DOI: 10.1074/jbc.m312719200
    tissue_or_cell_type
    Glutathionylated substrates

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 827–838

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human glutaredoxin kinetics and mutants · source_derived_draft · unverified_draft

    ### glutathione-glrx2-alternative-donor A thioredoxin-reductase/NADPH system reduced GLRX2 disulfide and GSH-GLRX2 intermediates. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutaredoxin recovery also had an alternative donor route in the assay. organism: Human GLRX1/GLRX2 tissue_or_cell_type: Glutathionylated substrates experimental_model: Purified human glutaredoxin kinetics and mutants limitations: Thioredoxin-reductase isoform is not assigned from the indexed abstract; this is not a new selenium-dose response. exposure: GSH or NADPH/thioredoxin-reductase donor systems evidence_span: {"source_cache": "artifacts/glutathione-research/14676218.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84", "start_char": 0, "end_char": 1398, "text_sha256": "a7399b7d035bd3815c30362449b7986dea08873c824e05506d7db627a71daa84"} [glutathione-p14676218] Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. (2004). https://pubmed.ncbi.nlm.nih.gov/14676218/ DOI: 10.1074/jbc.m312719200
    Complete structured claim and evidence

  2. Apo-GLRX5 reduced glutathione mixed disulfides about 100 times more slowly than GLRX2.

    Human mitochondrial glutaredoxin 5 / GLRX5 → Human glutaredoxin 2 / GLRX2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/21029046.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2", "start_char": 0, "end_char": 1468, "text_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2"}
    experimental_model
    Crystallography, solution oligomers and biochemical assays
    exposure
    Iron-sulfur/GSH complex and disulfide assays
    limitations
    The structural cluster complex is not a dietary-iron requirement or proof of supplement synergy.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human GLRX5
    plain_language
    Related glutaredoxins are not functionally interchangeable.
    primary_references
    [glutathione-p21029046] The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity. (2011). https://pubmed.ncbi.nlm.nih.gov/21029046/ DOI: 10.1042/bj20101286
    tissue_or_cell_type
    Purified holo and apo protein

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 801–812

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystallography, solution oligomers and biochemical assays · source_derived_draft · unverified_draft

    ### glutathione-glrx5-disulfide-rate Apo-GLRX5 reduced glutathione mixed disulfides about 100 times more slowly than GLRX2. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Related glutaredoxins are not functionally interchangeable. organism: Human GLRX5 tissue_or_cell_type: Purified holo and apo protein experimental_model: Crystallography, solution oligomers and biochemical assays limitations: The structural cluster complex is not a dietary-iron requirement or proof of supplement synergy. exposure: Iron-sulfur/GSH complex and disulfide assays evidence_span: {"source_cache": "artifacts/glutathione-research/21029046.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2", "start_char": 0, "end_char": 1468, "text_sha256": "bc7e33127eee3685d1f90bff5a83334d68ac0ee3f73eeb67e4a9e189c5ba20b2"} [glutathione-p21029046] The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity. (2011). https://pubmed.ncbi.nlm.nih.gov/21029046/ DOI: 10.1042/bj20101286
    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