Component

Thioredoxin reductase truncated of its C-terminal SeCys-Gly dipeptide, the form expected in selenium deficiency

Thioredoxin reductase truncated of its C-terminal SeCys-Gly dipeptide, the form expected in selenium deficiency. Species, exposure and limitations are retained in each linked claim.

1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

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What it does

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Recorded relationships

What it acts on

  1. Whereas hydrogen peroxide was a substrate for the wild-type enzyme, all mutant enzymes, including the truncated form expected in selenium deficiency, lacked hydroperoxidase activity, so selenium is required for the catalytic activities of thioredoxin reductase.

    Thioredoxin reductase truncated of its C-terminal SeCys-Gly dipeptide, the form expected in selenium deficiency → Thioredoxin reductase hydroperoxidase activity toward hydrogen peroxide source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/hbot-research/10849437.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13fe79ebefbddac9a76f4cae2e0f1aede8d648b6568adca72f0b0a550e66bc90", "start_char": 0, "end_char": 1374, "text_sha256": "13fe79ebefbddac9a76f4cae2e0f1aede8d648b6568adca72f0b0a550e66bc90"}
    experimental_model
    Recombinant rat thioredoxin reductase with selenocysteine mutations expressed in E. coli
    exposure
    SeCys498 replaced by cysteine or serine, and a truncated protein lacking the C-terminal SeCys-Gly dipeptide
    limitations
    The truncated construct is described by the authors as the form expected in selenium deficiency, which is what links this enzyme chemistry to nutrient supply. It remains a recombinant model, not a measurement in a selenium-deficient animal.
    nutrient_topic
    Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. · Hyperbaric oxygen therapy
    organism
    Rat enzyme in a bacterial expression host
    plain_language
    Without selenium the enzyme can no longer destroy peroxide at all.
    primary_references
    [hbot-p10849437] Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. (2000). https://pubmed.ncbi.nlm.nih.gov/10849437/ DOI: 10.1074/jbc.m000690200
    tissue_or_cell_type
    Purified enzyme
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Hyperbaric oxygen: the exposure, its reactive species, the signals they carry, and the nutrient-dependent enzymes that handle them (2026-09-19) · lines 478–489

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant rat thioredoxin reductase with selenocysteine mutations expressed in E. coli · source_derived_draft · unverified_draft

    ### hbot-trxr-truncated-no-activity Whereas hydrogen peroxide was a substrate for the wild-type enzyme, all mutant enzymes, including the truncated form expected in selenium deficiency, lacked hydroperoxidase activity, so selenium is required for the catalytic activities of thioredoxin reductase. Condition category: nutrient_deficiency nutrient_topic: Hyperbaric oxygen research collection; topical membership is not evidence of a direct clinical effect, and a therapeutic exposure is not a dietary intake. plain_language: Without selenium the enzyme can no longer destroy peroxide at all. organism: Rat enzyme in a bacterial expression host tissue_or_cell_type: Purified enzyme experimental_model: Recombinant rat thioredoxin reductase with selenocysteine mutations expressed in E. coli limitations: The truncated construct is described by the authors as the form expected in selenium deficiency, which is what links this enzyme chemistry to nutrient supply. It remains a recombinant model, not a measurement in a selenium-deficient animal. exposure: SeCys498 replaced by cysteine or serine, and a truncated protein lacking the C-terminal SeCys-Gly dipeptide evidence_span: {"source_cache": "artifacts/hbot-research/10849437.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "13fe79ebefbddac9a76f4cae2e0f1aede8d648b6568adca72f0b0a550e66bc90", "start_char": 0, "end_char": 1374, "text_sha256": "13fe79ebefbddac9a76f4cae2e0f1aede8d648b6568adca72f0b0a550e66bc90"} [hbot-p10849437] Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. (2000). https://pubmed.ncbi.nlm.nih.gov/10849437/ DOI: 10.1074/jbc.m000690200
    Complete structured claim and evidence

In the sources

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