Component

Gamma-glutamylcysteine

Gamma-glutamylcysteine. Species, exposure and limitations are retained in each linked claim.

5 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. Glutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine in the first glutathione-synthesis step.

    Human glutamate-cysteine ligase catalytic subunit / GCLC → Gamma-glutamylcysteine 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": 762, "end_char": 1092, "text_sha256": "927fa13b085700c20b578ecabc7c8c17a66ea4600b90809e3061d12bcaea3849"}
    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 machinery still needs its amino-acid building blocks.
    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 840–851

    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-gcl-first-step Glutamate-cysteine ligase joins glutamate and cysteine to form gamma-glutamylcysteine in the first glutathione-synthesis step. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The induced machinery still needs its amino-acid building blocks. 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": 762, "end_char": 1092, "text_sha256": "927fa13b085700c20b578ecabc7c8c17a66ea4600b90809e3061d12bcaea3849"} [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. The described Mycobacterium smegmatis pathway uses EgtA to condense glutamate and cysteine into gamma-glutamylcysteine.

    Mycobacterium smegmatis EgtA → Gamma-glutamylcysteine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text, pathway background citing original reconstitution
    experimental_model
    Pathway description in the primary EgtE paper, citing the original reconstitution.
    limitations
    This step is cited background, not a new EgtA experiment in this paper; microbial and human pathways remain separate.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    A separately encoded enzyme prepares the sulfur donor.
    primary_references
    Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26149121/ · DOI 10.1038/srep11870

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 560–566

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Pathway description in the primary EgtE paper, citing the original reconstitution. · source_derived_draft · unverified_draft

    ## ergothioneine-egta-precursor A separately encoded enzyme prepares the sulfur donor. The described Mycobacterium smegmatis pathway uses EgtA to condense glutamate and cysteine into gamma-glutamylcysteine. Model: Pathway description in the primary EgtE paper, citing the original reconstitution. Limitations: This step is cited background, not a new EgtA experiment in this paper; microbial and human pathways remain separate. Evidence access: Primary full text, pathway background citing original reconstitution Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26149121/ · DOI 10.1038/srep11870
    Complete structured claim and evidence

  3. Mycobacterium thermoresistibile EgtB coupled gamma-glutamylcysteine to hercynine through an oxygen-dependent C-S bond-forming reaction.

    Mycobacterium thermoresistibile EgtB → Gamma-glutamylcysteine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Crystal structure and enzyme mechanism study.
    limitations
    Non-heme iron coordination supports a proposed radical mechanism, not direct observation of every intermediate.
    nutrient_topic
    Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Ergothioneine
    plain_language
    A cysteine-containing precursor supplies sulfur.
    primary_references
    Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25597398/ · DOI 10.1002/anie.201410045

    Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 184–190

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Crystal structure and enzyme mechanism study. · source_derived_draft · unverified_draft

    ## ergothioneine-egtb-sulfur-donor A cysteine-containing precursor supplies sulfur. Mycobacterium thermoresistibile EgtB coupled gamma-glutamylcysteine to hercynine through an oxygen-dependent C-S bond-forming reaction. Model: Crystal structure and enzyme mechanism study. Limitations: Non-heme iron coordination supports a proposed radical mechanism, not direct observation of every intermediate. Evidence access: Primary abstract Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25597398/ · DOI 10.1002/anie.201410045
    Complete structured claim and evidence

Where it participates (unsigned role)

  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

  2. The lesion localized to GSS; findings supported excess gamma-glutamylcysteine-derived 5-oxoproline production beyond disposal capacity.

    GSS-deficient tissues from the two sisters studied in 1974 → 5-Oxoproline overproduction and urinary excretion in inherited GSS deficiency source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/glutathione-research/4152248.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "67120c198b8519f539205ac8148f02ffaf3ae37dc26810a7181cb18887db51d5", "start_char": 0, "end_char": 750, "text_sha256": "67120c198b8519f539205ac8148f02ffaf3ae37dc26810a7181cb18887db51d5"}
    experimental_model
    Enzyme studies in two affected sisters
    exposure
    Inherited 5-oxoprolinuria
    limitations
    Small historical disease study; overproduction mechanism is the authors’ interpretation, not a universal cause of acidosis.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human
    plain_language
    A blocked assembly pathway can also accumulate a side product.
    primary_references
    [glutathione-p4152248] Glutathione synthetase deficiency, an inborn error of metabolism involving the gamma-glutamyl cycle in patients with 5-oxoprolinuria (pyroglutamic aciduria). (1974). https://pubmed.ncbi.nlm.nih.gov/4152248/ DOI: 10.1073/pnas.71.6.2505
    tissue_or_cell_type
    Placenta, fibroblasts and erythrocytes
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 437–448

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Enzyme studies in two affected sisters · source_derived_draft · unverified_draft

    ### glutathione-gss-pyroglutamate The lesion localized to GSS; findings supported excess gamma-glutamylcysteine-derived 5-oxoproline production beyond disposal capacity. Condition category: machinery_impairment nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: A blocked assembly pathway can also accumulate a side product. organism: Human tissue_or_cell_type: Placenta, fibroblasts and erythrocytes experimental_model: Enzyme studies in two affected sisters limitations: Small historical disease study; overproduction mechanism is the authors’ interpretation, not a universal cause of acidosis. exposure: Inherited 5-oxoprolinuria evidence_span: {"source_cache": "artifacts/glutathione-research/4152248.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "67120c198b8519f539205ac8148f02ffaf3ae37dc26810a7181cb18887db51d5", "start_char": 0, "end_char": 750, "text_sha256": "67120c198b8519f539205ac8148f02ffaf3ae37dc26810a7181cb18887db51d5"} [glutathione-p4152248] Glutathione synthetase deficiency, an inborn error of metabolism involving the gamma-glutamyl cycle in patients with 5-oxoprolinuria (pyroglutamic aciduria). (1974). https://pubmed.ncbi.nlm.nih.gov/4152248/ DOI: 10.1073/pnas.71.6.2505
    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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