Component
Human glutathione-specific gamma-glutamylcyclotransferase CHAC2
Human glutathione-specific gamma-glutamylcyclotransferase CHAC2. 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 it acts on
Purified human CHAC2 degraded reduced GSH with lower catalytic efficiency than CHAC1.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/glutathione-research/27913623.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ddf397c2cb8fd60423c89cab28a0b54d124f0e34e0564a32d6bca36841530694", "start_char": 0, "end_char": 1617, "text_sha256": "ddf397c2cb8fd60423c89cab28a0b54d124f0e34e0564a32d6bca36841530694"}
- experimental_model
- Purified mammalian enzymes and expression comparison
- exposure
- CHAC1/CHAC2 substrate and kinetics comparison
- limitations
- Human kinetics and yeast structure are distinct; this does not establish a universal turnover rate in vivo.
- nutrient_topic
- Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
- organism
- Human and mouse enzymes; yeast structural homolog
- plain_language
- A separate enzyme supports slower glutathione turnover.
- primary_references
- [glutathione-p27913623] ChaC2, an Enzyme for Slow Turnover of Cytosolic Glutathione. (2017). https://pubmed.ncbi.nlm.nih.gov/27913623/ DOI: 10.1074/jbc.m116.727479
- tissue_or_cell_type
- Cytosolic glutathione turnover
Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 593–604
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian enzymes and expression comparison · source_derived_draft · unverified_draft
### glutathione-chac2-gsh Purified human CHAC2 degraded reduced GSH with lower catalytic efficiency than CHAC1. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: A separate enzyme supports slower glutathione turnover. organism: Human and mouse enzymes; yeast structural homolog tissue_or_cell_type: Cytosolic glutathione turnover experimental_model: Purified mammalian enzymes and expression comparison limitations: Human kinetics and yeast structure are distinct; this does not establish a universal turnover rate in vivo. exposure: CHAC1/CHAC2 substrate and kinetics comparison evidence_span: {"source_cache": "artifacts/glutathione-research/27913623.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ddf397c2cb8fd60423c89cab28a0b54d124f0e34e0564a32d6bca36841530694", "start_char": 0, "end_char": 1617, "text_sha256": "ddf397c2cb8fd60423c89cab28a0b54d124f0e34e0564a32d6bca36841530694"} [glutathione-p27913623] ChaC2, an Enzyme for Slow Turnover of Cytosolic Glutathione. (2017). https://pubmed.ncbi.nlm.nih.gov/27913623/ DOI: 10.1074/jbc.m116.727479
Complete structured claim and evidenceCHAC2 showed no activity against oxidized glutathione in the substrate comparison.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/glutathione-research/27913623.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ddf397c2cb8fd60423c89cab28a0b54d124f0e34e0564a32d6bca36841530694", "start_char": 0, "end_char": 1617, "text_sha256": "ddf397c2cb8fd60423c89cab28a0b54d124f0e34e0564a32d6bca36841530694"}
- experimental_model
- Purified mammalian enzymes and expression comparison
- exposure
- CHAC1/CHAC2 substrate and kinetics comparison
- limitations
- Human kinetics and yeast structure are distinct; this does not establish a universal turnover rate in vivo.
- nutrient_topic
- Glutathione research collection; topical membership is not evidence of a direct dietary effect. · GSH
- organism
- Human and mouse enzymes; yeast structural homolog
- plain_language
- Reduced and oxidized glutathione were not interchangeable substrates.
- primary_references
- [glutathione-p27913623] ChaC2, an Enzyme for Slow Turnover of Cytosolic Glutathione. (2017). https://pubmed.ncbi.nlm.nih.gov/27913623/ DOI: 10.1074/jbc.m116.727479
- tissue_or_cell_type
- Cytosolic glutathione turnover
Glutathione: metabolism, signaling and nutrient connections (2026-09-17) · lines 606–617
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified mammalian enzymes and expression comparison · source_derived_draft · unverified_draft
### glutathione-chac2-gssg-null CHAC2 showed no activity against oxidized glutathione in the substrate comparison. Condition category: normal nutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect. plain_language: Reduced and oxidized glutathione were not interchangeable substrates. organism: Human and mouse enzymes; yeast structural homolog tissue_or_cell_type: Cytosolic glutathione turnover experimental_model: Purified mammalian enzymes and expression comparison limitations: Human kinetics and yeast structure are distinct; this does not establish a universal turnover rate in vivo. exposure: CHAC1/CHAC2 substrate and kinetics comparison evidence_span: {"source_cache": "artifacts/glutathione-research/27913623.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ddf397c2cb8fd60423c89cab28a0b54d124f0e34e0564a32d6bca36841530694", "start_char": 0, "end_char": 1617, "text_sha256": "ddf397c2cb8fd60423c89cab28a0b54d124f0e34e0564a32d6bca36841530694"} [glutathione-p27913623] ChaC2, an Enzyme for Slow Turnover of Cytosolic Glutathione. (2017). https://pubmed.ncbi.nlm.nih.gov/27913623/ DOI: 10.1074/jbc.m116.727479
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.