Component

S-Nitrosoglutathione / GSNO

S-Nitrosoglutathione / GSNO. 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. GSNO treatment S-nitrosated human mitochondrial ThrRS and reduced both aminoacylation and editing activity in vitro.

    S-Nitrosoglutathione / GSNO → Human mitochondrial threonyl-tRNA synthetase / TARS2 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Purified human enzyme; four modified cysteine residues; corroborating S-nitrosation detection in human cells and mouse tissues.
    limitations
    GSNO is not reduced glutathione; this exposure does not predict effects of oral glutathione. H2O2 resistance and GSNO sensitivity were distinct in this study.
    nutrient_topic
    L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
    plain_language
    Chemical modification of the enzyme can disrupt loading and proofreading.
    primary_references
    Nitrosative stress inhibits aminoacylation and editing activities of mitochondrial threonyl-tRNA synthetase by S-nitrosation. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32484546/ · DOI 10.1093/nar/gkaa471
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 90–96

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human enzyme; four modified cysteine residues; corroborating S-nitrosation detection in human cells and mouse tissues. · source_derived_draft · unverified_draft

    ## l-threonine-tars2-nitrosation Chemical modification of the enzyme can disrupt loading and proofreading. GSNO treatment S-nitrosated human mitochondrial ThrRS and reduced both aminoacylation and editing activity in vitro. Model: Purified human enzyme; four modified cysteine residues; corroborating S-nitrosation detection in human cells and mouse tissues. Limitations: GSNO is not reduced glutathione; this exposure does not predict effects of oral glutathione. H2O2 resistance and GSNO sensitivity were distinct in this study. Evidence access: Primary abstract Nitrosative stress inhibits aminoacylation and editing activities of mitochondrial threonyl-tRNA synthetase by S-nitrosation. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32484546/ · DOI 10.1093/nar/gkaa471
    Complete structured claim and evidence

What acts on it

  1. The activity purified from mouse macrophages metabolized GSNO and was identified as glutathione-dependent formaldehyde dehydrogenase.

    Mouse S-nitrosoglutathione reductase / Adh5 → S-Nitrosoglutathione / GSNO source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/11260719.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "37ea7e3741c139cea0718d0cdf5e81da638a0f67269277289aa3f715e4c5df61", "start_char": 0, "end_char": 1177, "text_sha256": "37ea7e3741c139cea0718d0cdf5e81da638a0f67269277289aa3f715e4c5df61"}
    experimental_model
    Purification and genetic deletion
    exposure
    GSNO-consuming enzyme identification and deletion
    limitations
    The mouse gene is kept separate from human ADH5. Protein SNO regulation is not identical to direct peroxide removal.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Bacteria, yeast and mouse; mouse findings separated
    plain_language
    A glutathione derivative links to nitric-oxide-related signaling.
    primary_references
    [glutathione-p11260719] A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. (2001). https://pubmed.ncbi.nlm.nih.gov/11260719/ DOI: 10.1038/35068596
    tissue_or_cell_type
    Cellular nitrosothiol metabolism

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 996–1007

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purification and genetic deletion · source_derived_draft · unverified_draft

    ### glutathione-gsnor-gsno The activity purified from mouse macrophages metabolized GSNO and was identified as glutathione-dependent formaldehyde dehydrogenase. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: A glutathione derivative links to nitric-oxide-related signaling. organism: Bacteria, yeast and mouse; mouse findings separated tissue_or_cell_type: Cellular nitrosothiol metabolism experimental_model: Purification and genetic deletion limitations: The mouse gene is kept separate from human ADH5. Protein SNO regulation is not identical to direct peroxide removal. exposure: GSNO-consuming enzyme identification and deletion evidence_span: {"source_cache": "artifacts/glutathione-research/11260719.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "37ea7e3741c139cea0718d0cdf5e81da638a0f67269277289aa3f715e4c5df61", "start_char": 0, "end_char": 1177, "text_sha256": "37ea7e3741c139cea0718d0cdf5e81da638a0f67269277289aa3f715e4c5df61"} [glutathione-p11260719] A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. (2001). https://pubmed.ncbi.nlm.nih.gov/11260719/ DOI: 10.1038/35068596
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Reductase deletion increased protein SNO as well as GSNO in the studied mouse system.

    Adh5-null mouse cells in the 2001 study → Mouse intracellular protein S-nitrosylation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/glutathione-research/11260719.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "37ea7e3741c139cea0718d0cdf5e81da638a0f67269277289aa3f715e4c5df61", "start_char": 0, "end_char": 1177, "text_sha256": "37ea7e3741c139cea0718d0cdf5e81da638a0f67269277289aa3f715e4c5df61"}
    experimental_model
    Purification and genetic deletion
    exposure
    GSNO-consuming enzyme identification and deletion
    limitations
    The mouse gene is kept separate from human ADH5. Protein SNO regulation is not identical to direct peroxide removal.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Bacteria, yeast and mouse; mouse findings separated
    plain_language
    Changing the small-molecule pool affected protein modifications.
    primary_references
    [glutathione-p11260719] A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. (2001). https://pubmed.ncbi.nlm.nih.gov/11260719/ DOI: 10.1038/35068596
    tissue_or_cell_type
    Cellular nitrosothiol metabolism
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 1009–1020

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purification and genetic deletion · source_derived_draft · unverified_draft

    ### glutathione-gsnor-protein-sno Reductase deletion increased protein SNO as well as GSNO in the studied mouse system. Condition category: machinery_impairment nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Changing the small-molecule pool affected protein modifications. organism: Bacteria, yeast and mouse; mouse findings separated tissue_or_cell_type: Cellular nitrosothiol metabolism experimental_model: Purification and genetic deletion limitations: The mouse gene is kept separate from human ADH5. Protein SNO regulation is not identical to direct peroxide removal. exposure: GSNO-consuming enzyme identification and deletion evidence_span: {"source_cache": "artifacts/glutathione-research/11260719.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "37ea7e3741c139cea0718d0cdf5e81da638a0f67269277289aa3f715e4c5df61", "start_char": 0, "end_char": 1177, "text_sha256": "37ea7e3741c139cea0718d0cdf5e81da638a0f67269277289aa3f715e4c5df61"} [glutathione-p11260719] A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. (2001). https://pubmed.ncbi.nlm.nih.gov/11260719/ DOI: 10.1038/35068596
    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