Glutathione-Related Enzymes and Proteins: A Review

Overview

Journal Molecules

Publisher MDPI

Specialty Biology

Date 2023 Feb 11

PMID 36771108

Authors

Janka Vaskova

Ladislav Kocan

Ladislav Vasko

Pal Perjesi

Affiliations

Soon will be listed here.

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.

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