Immune
Glutathione
Endogenous Tripeptide
- γ-linked tripeptide
Scientific Overview
Glutathione is a tripeptide of glutamate, cysteine, and glycine found in most cells. Research literature covers its synthesis, its role in cellular redox balance, and its use as a substrate for thiol-dependent enzymes.
Mechanism focus
Synthesis is controlled largely through glutamate-cysteine ligase and glutathione synthetase. The tripeptide participates in thiol-disulfide exchange and is a cofactor for glutathione peroxidases and transferases.
Research Use Cases
- Cellular redox assays
- Glutathione synthesis pathway research
- Thiol-dependent enzyme studies
- Measurement of reduced and oxidized glutathione
Use-Case Study Notations
- Case-study notation: biosynthesis reviews describe the two-step synthesis of the tripeptide and its regulation.
- Case-study notation: metabolism reviews place glutathione in cellular redox systems rather than in a single pathway.
- This page is a research overview of the molecule. It does not present clinical outcome claims.
Selected Studies
- 01 Glutathione: overview of its protective roles, measurement, and biosynthesisPubMed 18796312
- 02 Glutathione synthesisPubMed 22995213
- 03 Glutathione metabolism and its implications for healthPubMed 14988435
- 04 Glutathione metabolism and its selective modificationPubMed 3053703
- 05 The importance of glutathione in human diseasePubMed 12818476
Related compounds
Research Use Only. This page is educational and intended for laboratory research context. Products are not for human consumption and are not intended to diagnose, treat, cure, or prevent any disease.