Component

Human glutamate-cysteine ligase catalytic activity

Human glutamate-cysteine ligase catalytic activity. 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 human GCL holoenzyme was more active and less sensitive to glutathione inhibition than its catalytic subunit alone.

    Human glutamate-cysteine ligase modifier subunit / GCLM → Human glutamate-cysteine ligase catalytic activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"}
    experimental_model
    Purified recombinant subunit/holoenzyme kinetics
    exposure
    Substrate comparisons and glutathione inhibition
    limitations
    Baseline enzymology, not a sulforaphane or nutrient-repletion trial.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Human GCLC and GCLM expressed in insect cells
    plain_language
    The modifier subunit changes how the glutathione-building enzyme works.
    primary_references
    [sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
    tissue_or_cell_type
    Glutathione synthesis first-step enzyme

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 814–825

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant subunit/holoenzyme kinetics · source_derived_draft · unverified_draft

    ### sulforaphane-gclm-activity The human GCL holoenzyme was more active and less sensitive to glutathione inhibition than its catalytic subunit alone. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The modifier subunit changes how the glutathione-building enzyme works. organism: Human GCLC and GCLM expressed in insect cells tissue_or_cell_type: Glutathione synthesis first-step enzyme experimental_model: Purified recombinant subunit/holoenzyme kinetics limitations: Baseline enzymology, not a sulforaphane or nutrient-repletion trial. exposure: Substrate comparisons and glutathione inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"} [sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
    Complete structured claim and evidence

  2. Glutathione inhibited both human GCLC and GCL holoenzyme, with greater sensitivity of GCLC alone.

    GSH → Human glutamate-cysteine ligase catalytic activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"}
    experimental_model
    Purified recombinant subunit/holoenzyme kinetics
    exposure
    Substrate comparisons and glutathione inhibition
    limitations
    Baseline enzymology, not a sulforaphane or nutrient-repletion trial.
    nutrient_topic
    Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. · Sulforaphane / SFN, stereochemistry specified per study
    organism
    Human GCLC and GCLM expressed in insect cells
    plain_language
    The product feeds back on the machinery that makes more of it.
    primary_references
    [sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
    tissue_or_cell_type
    Glutathione synthesis first-step enzyme

    Sulforaphane: formation, electrophile sensing and nutrient connections (2026-09-17) · lines 827–838

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant subunit/holoenzyme kinetics · source_derived_draft · unverified_draft

    ### sulforaphane-gsh-feedback Glutathione inhibited both human GCLC and GCL holoenzyme, with greater sensitivity of GCLC alone. Condition category: normal nutrient_topic: Sulforaphane research collection; topical membership is not evidence of a direct dietary effect. plain_language: The product feeds back on the machinery that makes more of it. organism: Human GCLC and GCLM expressed in insect cells tissue_or_cell_type: Glutathione synthesis first-step enzyme experimental_model: Purified recombinant subunit/holoenzyme kinetics limitations: Baseline enzymology, not a sulforaphane or nutrient-repletion trial. exposure: Substrate comparisons and glutathione inhibition evidence_span: {"source_cache": "artifacts/sulforaphane-research/9637733.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2", "start_char": 0, "end_char": 1258, "text_sha256": "4e7a66b2c4a636f70f2a5954ff304e54d4ef0f00055e53bc32ba8ceb9772fbe2"} [sulforaphane-p9637733] Expression and characterization of human glutamate-cysteine ligase. (1998). https://pubmed.ncbi.nlm.nih.gov/9637733/ DOI: 10.1006/abbi.1998.0676
    Complete structured claim and evidence

  3. Adding GCLM largely rescued impaired activity of recombinant GCLC Arg127Cys, His370Leu and Pro414Leu.

    Human glutamate-cysteine ligase modifier subunit / GCLM → Human glutamate-cysteine ligase catalytic activity source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/glutathione-research/21657237.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0ef7f04eacc64f48cee159ed630014f38163f2b848bf36b99c4d371786f55d7", "start_char": 0, "end_char": 1854, "text_sha256": "d0ef7f04eacc64f48cee159ed630014f38163f2b848bf36b99c4d371786f55d7"}
    experimental_model
    Human variants in recombinant assays, mouse fibroblasts and yeast complementation
    exposure
    Four clinical GCLC variants with or without GCLM
    limitations
    Expression-system rescue does not establish a clinical therapy; Pro158Leu retains near-wild-type isolated kinetics.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human GCLC/GCLM; mouse and yeast hosts
    plain_language
    The partner subunit changed how a damaged catalytic subunit performed.
    primary_references
    [glutathione-p21657237] Enzymatic defects underlying hereditary glutamate cysteine ligase deficiency are mitigated by association of the catalytic and regulatory subunits. (2011). https://pubmed.ncbi.nlm.nih.gov/21657237/ DOI: 10.1021/bi200708w
    tissue_or_cell_type
    GCL activity and cellular GSH
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 398–409

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human variants in recombinant assays, mouse fibroblasts and yeast complementation · source_derived_draft · unverified_draft

    ### glutathione-gclm-mutant-rescue Adding GCLM largely rescued impaired activity of recombinant GCLC Arg127Cys, His370Leu and Pro414Leu. Condition category: machinery_impairment nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The partner subunit changed how a damaged catalytic subunit performed. organism: Human GCLC/GCLM; mouse and yeast hosts tissue_or_cell_type: GCL activity and cellular GSH experimental_model: Human variants in recombinant assays, mouse fibroblasts and yeast complementation limitations: Expression-system rescue does not establish a clinical therapy; Pro158Leu retains near-wild-type isolated kinetics. exposure: Four clinical GCLC variants with or without GCLM evidence_span: {"source_cache": "artifacts/glutathione-research/21657237.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d0ef7f04eacc64f48cee159ed630014f38163f2b848bf36b99c4d371786f55d7", "start_char": 0, "end_char": 1854, "text_sha256": "d0ef7f04eacc64f48cee159ed630014f38163f2b848bf36b99c4d371786f55d7"} [glutathione-p21657237] Enzymatic defects underlying hereditary glutamate cysteine ligase deficiency are mitigated by association of the catalytic and regulatory subunits. (2011). https://pubmed.ncbi.nlm.nih.gov/21657237/ DOI: 10.1021/bi200708w
    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