Component

Saccharomyces cerevisiae glutamate-cysteine ligase Gsh1

Saccharomyces cerevisiae glutamate-cysteine ligase Gsh1. 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 acts on it

  1. The bound BSO inhibitory species was phosphorylated on its sulfoximine nitrogen.

    L-Buthionine-S-sulfoximine / BSO → Saccharomyces cerevisiae glutamate-cysteine ligase Gsh1 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/glutathione-research/20220146.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478", "start_char": 0, "end_char": 1382, "text_sha256": "c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478"}
    experimental_model
    Inhibited-enzyme crystallography
    exposure
    GSH and BSO-bound structures
    limitations
    Binding geometry is species-specific; BSO is an experimental inhibitor, not dietary depletion.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Saccharomyces cerevisiae
    plain_language
    The inhibitor is chemically activated at the enzyme.
    primary_references
    [glutathione-p20220146] Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase. (2010). https://pubmed.ncbi.nlm.nih.gov/20220146/ DOI: 10.1074/jbc.m110.104802
    tissue_or_cell_type
    Purified Gsh1
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 372–383

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

    ### glutathione-bso-gcl The bound BSO inhibitory species was phosphorylated on its sulfoximine nitrogen. Condition category: machinery_impairment nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The inhibitor is chemically activated at the enzyme. organism: Saccharomyces cerevisiae tissue_or_cell_type: Purified Gsh1 experimental_model: Inhibited-enzyme crystallography limitations: Binding geometry is species-specific; BSO is an experimental inhibitor, not dietary depletion. exposure: GSH and BSO-bound structures evidence_span: {"source_cache": "artifacts/glutathione-research/20220146.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478", "start_char": 0, "end_char": 1382, "text_sha256": "c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478"} [glutathione-p20220146] Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase. (2010). https://pubmed.ncbi.nlm.nih.gov/20220146/ DOI: 10.1074/jbc.m110.104802
    Complete structured claim and evidence

  2. GSH occupied the glutamate and presumed cysteine sites and disrupted ATP-site Mg coordination in the inhibited yeast structure.

    GSH → Saccharomyces cerevisiae glutamate-cysteine ligase Gsh1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/20220146.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478", "start_char": 0, "end_char": 1382, "text_sha256": "c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478"}
    experimental_model
    Inhibited-enzyme crystallography
    exposure
    GSH and BSO-bound structures
    limitations
    Binding geometry is species-specific; BSO is an experimental inhibitor, not dietary depletion.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Saccharomyces cerevisiae
    plain_language
    The product can feed back on its own synthesis.
    primary_references
    [glutathione-p20220146] Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase. (2010). https://pubmed.ncbi.nlm.nih.gov/20220146/ DOI: 10.1074/jbc.m110.104802
    tissue_or_cell_type
    Purified Gsh1

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 359–370

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

    ### glutathione-gcl-feedback-site GSH occupied the glutamate and presumed cysteine sites and disrupted ATP-site Mg coordination in the inhibited yeast structure. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The product can feed back on its own synthesis. organism: Saccharomyces cerevisiae tissue_or_cell_type: Purified Gsh1 experimental_model: Inhibited-enzyme crystallography limitations: Binding geometry is species-specific; BSO is an experimental inhibitor, not dietary depletion. exposure: GSH and BSO-bound structures evidence_span: {"source_cache": "artifacts/glutathione-research/20220146.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478", "start_char": 0, "end_char": 1382, "text_sha256": "c456343cb9386a797d12af2169106d7f3b8033a5fa3882034609d3bbc26ae478"} [glutathione-p20220146] Structural basis for feedback and pharmacological inhibition of Saccharomyces cerevisiae glutamate cysteine ligase. (2010). https://pubmed.ncbi.nlm.nih.gov/20220146/ DOI: 10.1074/jbc.m110.104802
    Complete structured claim and evidence

  3. The yeast GCL structures identified an ATP-independent magnesium coordination site associated with the enzyme’s Mg dependence.

    Mg2+ → Saccharomyces cerevisiae glutamate-cysteine ligase Gsh1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/19726687.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "fd125689fc03eaf0ec433fd6b967eecc6c52c234e99e3717f10218c2c4b97625", "start_char": 0, "end_char": 1461, "text_sha256": "fd125689fc03eaf0ec433fd6b967eecc6c52c234e99e3717f10218c2c4b97625"}
    experimental_model
    X-ray structures and human homology model
    exposure
    Glutamate/MgCl2 with or without ADP
    limitations
    Direct metal-site observation is yeast; the human model is an inference, not a human deficiency experiment.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Saccharomyces cerevisiae enzyme; separate human model
    plain_language
    Magnesium has a role beyond merely being present in the assay buffer.
    primary_references
    [glutathione-p19726687] Mechanistic details of glutathione biosynthesis revealed by crystal structures of Saccharomyces cerevisiae glutamate cysteine ligase. (2009). https://pubmed.ncbi.nlm.nih.gov/19726687/ DOI: 10.1074/jbc.m109.025114
    tissue_or_cell_type
    Purified Gsh1

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 346–357

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray structures and human homology model · source_derived_draft · unverified_draft

    ### glutathione-gcl-magnesium The yeast GCL structures identified an ATP-independent magnesium coordination site associated with the enzyme’s Mg dependence. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium has a role beyond merely being present in the assay buffer. organism: Saccharomyces cerevisiae enzyme; separate human model tissue_or_cell_type: Purified Gsh1 experimental_model: X-ray structures and human homology model limitations: Direct metal-site observation is yeast; the human model is an inference, not a human deficiency experiment. exposure: Glutamate/MgCl2 with or without ADP evidence_span: {"source_cache": "artifacts/glutathione-research/19726687.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "fd125689fc03eaf0ec433fd6b967eecc6c52c234e99e3717f10218c2c4b97625", "start_char": 0, "end_char": 1461, "text_sha256": "fd125689fc03eaf0ec433fd6b967eecc6c52c234e99e3717f10218c2c4b97625"} [glutathione-p19726687] Mechanistic details of glutathione biosynthesis revealed by crystal structures of Saccharomyces cerevisiae glutamate cysteine ligase. (2009). https://pubmed.ncbi.nlm.nih.gov/19726687/ DOI: 10.1074/jbc.m109.025114
    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.

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