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Updated: Jun 27, 2026

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases
Published on: October 10, 2020
Glutathione transferases in bacteria
Nerino Allocati1, Luca Federici, Michele Masulli
1Dipartimento di Scienze Biomediche, Università G. d'Annunzio, Chieti, Italy. allocati@unich.it
Bacterial glutathione transferases (GSTs) are crucial enzymes for detoxification in prokaryotes. This review covers their diverse functions, including xenobiotic biodegradation and stress protection.
Area of Science:
- Biochemistry
- Enzymology
- Microbiology
Background:
- Bacterial glutathione transferases (GSTs) are a superfamily of enzymes vital for cellular detoxification.
- GSTs are prevalent in prokaryotes and classified into distinct groups.
- They are involved in xenobiotic biodegradation, oxidative stress defense, and antimicrobial resistance.
Purpose of the Study:
- To review the current knowledge on the functional and structural properties of bacterial GSTs.
- To highlight the diverse roles of bacterial GSTs beyond detoxification.
Main Methods:
- Literature review of studies on bacterial glutathione transferases.
- Analysis of functional and structural data from various bacterial GSTs.
Main Results:
- Bacterial GSTs participate in diverse metabolic pathways, including the biotransformation of dichloromethane and degradation of pollutants like atrazine and pentachlorophenol.
- Their roles extend to protecting against chemical and oxidative stresses and contributing to antimicrobial drug resistance.
Conclusions:
- Bacterial GSTs are versatile enzymes with critical roles in cellular defense and metabolism.
- Further research into their structure-function relationships can unlock new biotechnological applications.
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