Component
S-D-Lactoylglutathione
S-D-Lactoylglutathione. Species, exposure and limitations are retained in each linked claim.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What acts on it
Human glyoxalase II hydrolyzes S-D-lactoylglutathione to GSH and D-lactate.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/glutathione-research/10508780.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2a3bc96920fd7c09bc46bfbdd6ade9698bb3dd421e0867023dec7679628d04eb", "start_char": 0, "end_char": 1432, "text_sha256": "2a3bc96920fd7c09bc46bfbdd6ade9698bb3dd421e0867023dec7679628d04eb"}
- experimental_model
- Crystal structures of free and ligand-bound GLO2
- exposure
- Thioester hydrolysis and substrate-analogue structure
- limitations
- The structure contained a binuclear zinc site; metal occupancy in this preparation is not a universal in-vivo metal assignment.
- nutrient_topic
- Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
- organism
- Human
- plain_language
- This clearance route regenerates glutathione instead of permanently consuming it.
- primary_references
- [glutathione-p10508780] Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. (1999). https://pubmed.ncbi.nlm.nih.gov/10508780/ DOI: 10.1016/s0969-2126(99)80174-9
- tissue_or_cell_type
- Purified glyoxalase II
Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 905–916
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structures of free and ligand-bound GLO2 · source_derived_draft · unverified_draft
### glutathione-glo2-recycles Human glyoxalase II hydrolyzes S-D-lactoylglutathione to GSH and D-lactate. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: This clearance route regenerates glutathione instead of permanently consuming it. organism: Human tissue_or_cell_type: Purified glyoxalase II experimental_model: Crystal structures of free and ligand-bound GLO2 limitations: The structure contained a binuclear zinc site; metal occupancy in this preparation is not a universal in-vivo metal assignment. exposure: Thioester hydrolysis and substrate-analogue structure evidence_span: {"source_cache": "artifacts/glutathione-research/10508780.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2a3bc96920fd7c09bc46bfbdd6ade9698bb3dd421e0867023dec7679628d04eb", "start_char": 0, "end_char": 1432, "text_sha256": "2a3bc96920fd7c09bc46bfbdd6ade9698bb3dd421e0867023dec7679628d04eb"} [glutathione-p10508780] Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. (1999). https://pubmed.ncbi.nlm.nih.gov/10508780/ DOI: 10.1016/s0969-2126(99)80174-9
Complete structured claim and evidence
Where it participates (unsigned role)
Human erythrocyte GLO1 forms S-D-lactoylglutathione through the methylglyoxal/GSH hemithioacetal intermediate.
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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.