Component

Human glyoxalase I / GLO1

Human glyoxalase I / GLO1. 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. Human GLO1 catalyzes glutathione-dependent methylglyoxal inactivation.

    Human glyoxalase I / GLO1 → Methylglyoxal source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/9218781.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1", "start_char": 0, "end_char": 1251, "text_sha256": "e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1"}
    experimental_model
    Human GLO1 crystal structure
    exposure
    S-benzyl-GSH complex
    limitations
    The essential zinc site is biochemical evidence; neither zinc nor GSH supplementation was tested.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human
    plain_language
    Glutathione also participates in handling a reactive carbonyl compound.
    primary_references
    [glutathione-p9218781] Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping. (1997). https://pubmed.ncbi.nlm.nih.gov/9218781/ DOI: 10.1093/emboj/16.12.3386
    tissue_or_cell_type
    Purified dimeric enzyme

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 879–890

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human GLO1 crystal structure · source_derived_draft · unverified_draft

    ### glutathione-glo1-methylglyoxal Human GLO1 catalyzes glutathione-dependent methylglyoxal inactivation. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Glutathione also participates in handling a reactive carbonyl compound. organism: Human tissue_or_cell_type: Purified dimeric enzyme experimental_model: Human GLO1 crystal structure limitations: The essential zinc site is biochemical evidence; neither zinc nor GSH supplementation was tested. exposure: S-benzyl-GSH complex evidence_span: {"source_cache": "artifacts/glutathione-research/9218781.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1", "start_char": 0, "end_char": 1251, "text_sha256": "e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1"} [glutathione-p9218781] Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping. (1997). https://pubmed.ncbi.nlm.nih.gov/9218781/ DOI: 10.1093/emboj/16.12.3386
    Complete structured claim and evidence

  2. Human erythrocyte GLO1 forms S-D-lactoylglutathione through the methylglyoxal/GSH hemithioacetal intermediate.

    Human glyoxalase I / GLO1 → Methylglyoxal-glutathione hemithioacetal source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/6863314.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "fc40fe8d31ed36ad75af255cf31121d46ab8905d456f4ff9d94cc857e6b0e00d", "start_char": 0, "end_char": 2097, "text_sha256": "fc40fe8d31ed36ad75af255cf31121d46ab8905d456f4ff9d94cc857e6b0e00d"}
    experimental_model
    Forward/reverse enzyme kinetics
    exposure
    Lactoyl-GSH and thiol-trapping experiments
    limitations
    Artificial trapping reveals reversibility; it does not reverse the usual physiological net flux.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human erythrocyte enzyme; separate yeast comparison
    plain_language
    The first enzyme supplies the substrate processed by glyoxalase II.
    primary_references
    [glutathione-p6863314] Reversal of the reaction catalyzed by glyoxalase I. Calculation of the equilibrium constant for the enzymatic reaction. (1983). https://pubmed.ncbi.nlm.nih.gov/6863314/ DOI: 10.1016/s0021-9258(18)32137-9
    tissue_or_cell_type
    Purified glyoxalase I

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 918–929

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

    ### glutathione-glo1-product Human erythrocyte GLO1 forms S-D-lactoylglutathione through the methylglyoxal/GSH hemithioacetal intermediate. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: The first enzyme supplies the substrate processed by glyoxalase II. organism: Human erythrocyte enzyme; separate yeast comparison tissue_or_cell_type: Purified glyoxalase I experimental_model: Forward/reverse enzyme kinetics limitations: Artificial trapping reveals reversibility; it does not reverse the usual physiological net flux. exposure: Lactoyl-GSH and thiol-trapping experiments evidence_span: {"source_cache": "artifacts/glutathione-research/6863314.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "fc40fe8d31ed36ad75af255cf31121d46ab8905d456f4ff9d94cc857e6b0e00d", "start_char": 0, "end_char": 2097, "text_sha256": "fc40fe8d31ed36ad75af255cf31121d46ab8905d456f4ff9d94cc857e6b0e00d"} [glutathione-p6863314] Reversal of the reaction catalyzed by glyoxalase I. Calculation of the equilibrium constant for the enzymatic reaction. (1983). https://pubmed.ncbi.nlm.nih.gov/6863314/ DOI: 10.1016/s0021-9258(18)32137-9
    Complete structured claim and evidence

What acts on it

  1. The human GLO1 active site contained an essential zinc ion with ligands contributed across the dimer interface.

    Zinc(II) ion → Human glyoxalase I / GLO1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/glutathione-research/9218781.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1", "start_char": 0, "end_char": 1251, "text_sha256": "e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1"}
    experimental_model
    Human GLO1 crystal structure
    exposure
    S-benzyl-GSH complex
    limitations
    The essential zinc site is biochemical evidence; neither zinc nor GSH supplementation was tested.
    nutrient_topic
    Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
    organism
    Human
    plain_language
    Zinc-dependent enzyme machinery connects to this glutathione pathway.
    primary_references
    [glutathione-p9218781] Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping. (1997). https://pubmed.ncbi.nlm.nih.gov/9218781/ DOI: 10.1093/emboj/16.12.3386
    tissue_or_cell_type
    Purified dimeric enzyme

    Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 892–903

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human GLO1 crystal structure · source_derived_draft · unverified_draft

    ### glutathione-glo1-zinc The human GLO1 active site contained an essential zinc ion with ligands contributed across the dimer interface. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Zinc-dependent enzyme machinery connects to this glutathione pathway. organism: Human tissue_or_cell_type: Purified dimeric enzyme experimental_model: Human GLO1 crystal structure limitations: The essential zinc site is biochemical evidence; neither zinc nor GSH supplementation was tested. exposure: S-benzyl-GSH complex evidence_span: {"source_cache": "artifacts/glutathione-research/9218781.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1", "start_char": 0, "end_char": 1251, "text_sha256": "e00867a8f693a2a0e6506a87d162a52ce4aa75ac846c7b0495dcf6ad7c9330e1"} [glutathione-p9218781] Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping. (1997). https://pubmed.ncbi.nlm.nih.gov/9218781/ DOI: 10.1093/emboj/16.12.3386
    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