Recent advances in protein engineering and biotechnological applications of glutathione transferases

Abstract

Glutathione transferases (GSTs, EC 2.5.1.18) are a widespread family of enzymes that play a central role in the detoxification, metabolism, and transport or sequestration of endogenous or xenobiotic compounds. During the last two decades, delineation of the important structural and catalytic features of GSTs has laid the groundwork for engineering GSTs, involving both rational and random approaches, aiming to create new variants with new or altered properties. These approaches have expanded the usefulness of native GSTs, not only for understanding the fundamentals of molecular detoxification mechanisms, but also for the development medical, analytical, environmental, and agricultural applications. This review article attempts to summarize successful examples and current developments on GST engineering, highlighting in parallel the recent knowledge gained on their phylogenetic relationships, structural/catalytic features, and biotechnological applications.

Keywords:

• Abiotic stress
• biotic stress
• enzyme engineering
• directed evolution
• glutathione transferase
• herbicide detoxification
• site-directed mutagenesis

Disclosure statement

The authors report no declarations of interest.

Additional information

Funding

This work was supported by the Research Projects for Excellence IKY/SIEMENS.