Component

Human glutathione synthetase / GSS

Human glutathione synthetase / GSS. Species, exposure and limitations are retained in each linked claim.

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 GSS joins gamma-glutamylcysteine and glycine in an ATP-dependent reaction to form glutathione.

    Human glutathione synthetase / GSS → GSH source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 923, "end_char": 1092, "text_sha256": "bed9ef1323b513b1e31b65277f28b935ddf0c9b0c83cbe9ee9f827f97806846c"}
    experimental_model
    Human enzyme mutagenesis, kinetics and molecular dynamics
    exposure
    S-loop variants; established biosynthetic reactions described in the introduction
    limitations
    Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Human GSS
    plain_language
    A second enzyme, glycine and energy complete the molecule.
    primary_references
    [sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
    tissue_or_cell_type
    Glutathione synthesis and substrate binding

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 853–864

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme mutagenesis, kinetics and molecular dynamics · source_derived_draft · unverified_draft

    ### sulforaphane-gss-second-step Human GSS joins gamma-glutamylcysteine and glycine in an ATP-dependent reaction to form glutathione. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second enzyme, glycine and energy complete the molecule. organism: Human GSS tissue_or_cell_type: Glutathione synthesis and substrate binding experimental_model: Human enzyme mutagenesis, kinetics and molecular dynamics limitations: Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency. exposure: S-loop variants; established biosynthetic reactions described in the introduction evidence_span: {"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 923, "end_char": 1092, "text_sha256": "bed9ef1323b513b1e31b65277f28b935ddf0c9b0c83cbe9ee9f827f97806846c"} [sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
    Complete structured claim and evidence

What acts on it

  1. The human GSS active sites bind ATP and associated magnesium for peptide-bond formation.

    Mg2+ → Human glutathione synthetase / GSS source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 1428, "end_char": 1604, "text_sha256": "a5d33b10162adea5e60fcff380eabf7e272963711914ea0e8e7091ad8c79df21"}
    experimental_model
    Human enzyme mutagenesis, kinetics and molecular dynamics
    exposure
    S-loop variants; established biosynthetic reactions described in the introduction
    limitations
    Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Human GSS
    plain_language
    The induced glutathione pathway still depends on ordinary enzyme cofactors.
    primary_references
    [sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
    tissue_or_cell_type
    Glutathione synthesis and substrate binding

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 866–877

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human enzyme mutagenesis, kinetics and molecular dynamics · source_derived_draft · unverified_draft

    ### sulforaphane-gss-magnesium The human GSS active sites bind ATP and associated magnesium for peptide-bond formation. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The induced glutathione pathway still depends on ordinary enzyme cofactors. organism: Human GSS tissue_or_cell_type: Glutathione synthesis and substrate binding experimental_model: Human enzyme mutagenesis, kinetics and molecular dynamics limitations: Reaction descriptions are background chemistry in a primary enzyme paper, not evidence that sulforaphane corrects inherited GSS deficiency. exposure: S-loop variants; established biosynthetic reactions described in the introduction evidence_span: {"source_cache": "artifacts/sulforaphane-research/30581542.fulltext.txt", "locator": "Primary full-text span; zero-based, end-exclusive Unicode character offsets", "file_sha256": "77cf6674cf9b9bc140a228588a53c937966fd3a67397c1c4970221c5cc58a0b1", "start_char": 1428, "end_char": 1604, "text_sha256": "a5d33b10162adea5e60fcff380eabf7e272963711914ea0e8e7091ad8c79df21"} [sulforaphane-p30581542] Genetic Mutations in the S-loop of Human Glutathione Synthetase: Links Between Substrate Binding, Active Site Structure and Allostery. (2019). https://pubmed.ncbi.nlm.nih.gov/30581542/ DOI: 10.1016/j.csbj.2018.11.008
    Complete structured claim and evidence

  2. Human GSS crystallized with two magnesium ions, ADP, glutathione and sulfate.

    Mg2+ → Human glutathione synthetase / GSS source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/10369661.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ccdd02e451ba6a6d432012c382911ff7fac556e99f9e8d60ce9f3dc94baf9941", "start_char": 0, "end_char": 1327, "text_sha256": "ccdd02e451ba6a6d432012c382911ff7fac556e99f9e8d60ce9f3dc94baf9941"}
    experimental_model
    Crystal structure and disease-variant mapping
    exposure
    ADP/GSH/sulfate-bound structure
    limitations
    Two Mg ions observed; structure is not a dietary-magnesium depletion experiment. The main synthesis reaction is reused from its existing claim.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human enzyme
    plain_language
    The synthesis enzyme has a metal-containing nucleotide-binding environment.
    primary_references
    [glutathione-p10369661] Molecular basis of glutathione synthetase deficiency and a rare gene permutation event. (1999). https://pubmed.ncbi.nlm.nih.gov/10369661/ DOI: 10.1093/emboj/18.12.3204
    tissue_or_cell_type
    Purified GSS

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 333–344

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structure and disease-variant mapping · source_derived_draft · unverified_draft

    ### glutathione-gss-magnesium Human GSS crystallized with two magnesium ions, ADP, glutathione and sulfate. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The synthesis enzyme has a metal-containing nucleotide-binding environment. organism: Human enzyme tissue_or_cell_type: Purified GSS experimental_model: Crystal structure and disease-variant mapping limitations: Two Mg ions observed; structure is not a dietary-magnesium depletion experiment. The main synthesis reaction is reused from its existing claim. exposure: ADP/GSH/sulfate-bound structure evidence_span: {"source_cache": "artifacts/glutathione-research/10369661.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ccdd02e451ba6a6d432012c382911ff7fac556e99f9e8d60ce9f3dc94baf9941", "start_char": 0, "end_char": 1327, "text_sha256": "ccdd02e451ba6a6d432012c382911ff7fac556e99f9e8d60ce9f3dc94baf9941"} [glutathione-p10369661] Molecular basis of glutathione synthetase deficiency and a rare gene permutation event. (1999). https://pubmed.ncbi.nlm.nih.gov/10369661/ DOI: 10.1093/emboj/18.12.3204
    Complete structured claim and evidence

  3. Peptide mapping identified NAPQI binding to GSS Cys422.

    N-Acetyl-p-benzoquinone imine / NAPQI → Human glutathione synthetase / GSS source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/glutathione-research/27086508.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3170945d1b6429e4d069dffe5fefd919b06714d7bea8a2b82d4b9eda916e9cad", "start_char": 0, "end_char": 1383, "text_sha256": "3170945d1b6429e4d069dffe5fefd919b06714d7bea8a2b82d4b9eda916e9cad"}
    experimental_model
    Mass spectrometry and in-vitro inhibition
    exposure
    0.77 micromolar enzyme with 25–400 micromolar NAPQI
    limitations
    Biological relevance and contribution to human 5-oxoprolinuric acidosis remain unproven.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human GSS preparation
    plain_language
    The reactive metabolite can attack synthesis machinery in vitro.
    primary_references
    [glutathione-p27086508] The acetaminophen metabolite N-acetyl-p-benzoquinone imine (NAPQI) inhibits glutathione synthetase in vitro; a clue to the mechanism of 5-oxoprolinuric acidosis? (2017). https://pubmed.ncbi.nlm.nih.gov/27086508/ DOI: 10.3109/00498254.2016.1166533
    tissue_or_cell_type
    Purified synthesis enzyme
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 1074–1085

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mass spectrometry and in-vitro inhibition · source_derived_draft · unverified_draft

    ### glutathione-napqi-gss-binding Peptide mapping identified NAPQI binding to GSS Cys422. Condition category: machinery_impairment nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The reactive metabolite can attack synthesis machinery in vitro. organism: Human GSS preparation tissue_or_cell_type: Purified synthesis enzyme experimental_model: Mass spectrometry and in-vitro inhibition limitations: Biological relevance and contribution to human 5-oxoprolinuric acidosis remain unproven. exposure: 0.77 micromolar enzyme with 25–400 micromolar NAPQI evidence_span: {"source_cache": "artifacts/glutathione-research/27086508.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3170945d1b6429e4d069dffe5fefd919b06714d7bea8a2b82d4b9eda916e9cad", "start_char": 0, "end_char": 1383, "text_sha256": "3170945d1b6429e4d069dffe5fefd919b06714d7bea8a2b82d4b9eda916e9cad"} [glutathione-p27086508] The acetaminophen metabolite N-acetyl-p-benzoquinone imine (NAPQI) inhibits glutathione synthetase in vitro; a clue to the mechanism of 5-oxoprolinuric acidosis? (2017). https://pubmed.ncbi.nlm.nih.gov/27086508/ DOI: 10.3109/00498254.2016.1166533
    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