Glutathione-Related Enzymes and Proteins: A Review

Molecules. 2023 Feb 2;28(3):1447. doi: 10.3390/molecules28031447.

Abstract

The tripeptide glutathione is found in all eukaryotic cells, and due to the compartmentalization of biochemical processes, its synthesis takes place exclusively in the cytosol. At the same time, its functions depend on its transport to/from organelles and interorgan transport, in which the liver plays a central role. Glutathione is determined as a marker of the redox state in many diseases, aging processes, and cell death resulting from its properties and reactivity. It also uses other enzymes and proteins, which enables it to engage and regulate various cell functions. This paper approximates the role of these systems in redox and detoxification reactions such as conjugation reactions of glutathione-S-transferases, glyoxylases, reduction of peroxides through thiol peroxidases (glutathione peroxidases, peroxiredoxins) and thiol-disulfide exchange reactions catalyzed by glutaredoxins.

Keywords: cell; glutathione; glutathione enzyme; glutathione system; glutathionylation; redox homeostasis.

Publication types

  • Review

MeSH terms

  • Glutaredoxins / metabolism
  • Glutathione Peroxidase / metabolism
  • Glutathione* / metabolism
  • Oxidation-Reduction
  • Proteins* / metabolism
  • Sulfhydryl Compounds / metabolism

Substances

  • Glutathione
  • Proteins
  • Glutathione Peroxidase
  • Sulfhydryl Compounds
  • Glutaredoxins

Grants and funding

This research received no external funding.