| Literature DB >> 28936894 |
Fereniki Perperopoulou1, Fotini Pouliou1, Nikolaos E Labrou1.
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.Entities:
Keywords: Abiotic stress; biotic stress; directed evolution; enzyme engineering; glutathione transferase; herbicide detoxification; site-directed mutagenesis
Mesh:
Substances:
Year: 2017 PMID: 28936894 DOI: 10.1080/07388551.2017.1375890
Source DB: PubMed Journal: Crit Rev Biotechnol ISSN: 0738-8551 Impact factor: 8.429