Stereoisomers of glutathione: preparation and enzymatic reactivities
Related Experiment Video
Updated: Oct 19, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
T Oikawa1, T Yamauchi, H Kumagai
1Department of Biotechnology, Faculty of Engineering, Kansai University, Osaka, Japan.
Abstract:
We synthesized a series of stereoisomers of glutathione (GSH) and glutathione disulfide (GSSG) by the solid-phase method. These peptides were used to examine their reactivities with enzymes acting on glutathione. The glutathione reductase of yeast acted only on LL-GSSG. Glutathione S-transferase catalyzed the conjugation of 1-chloro-2,4-dinitrobenzene with LL-GSH and DL-GSH (Km (mM): for LL-GSH, 0.035; and for DL-GSH, 0.62), but the DD- and LD-diastereomers were inert. gamma-Glutamyl transpeptidase catalyzed the transfer of gamma-glutamyl moiety of LL-GSH and DL-GSH to taurine forming gamma-glutamyl taurine and cysteinyl taurine (Km (mM): for LL-GSH, 0.336; and for DL-GSH, 0.628), but the other diastereomers were not the substrates. The occurrence of L-cysteinyl residue in the tripeptides is required for the glutathione analogue to be a substrate of the enzymes.
More Related Videos
Related Concept Videos
Phase II Reactions: Glutathione Conjugation and Mercapturic Acid Formation
Several distinctive characteristics distinguish glutathione conjugation from other phase II...
Prochirality
Preparation and Reactions of Thiols
Reactivity of Enols
Racemic Mixtures and the Resolution of Enantiomers
E1 Reaction: Stereochemistry and Regiochemistry

