A Glutathione Transferase from Agrobacterium tumefaciens Reveals a Novel Class of Bacterial GST Superfamily

Skopelitou, Katholiki; Dhavala, Prathusha; Papageorgiou, Anastassios C.; Labrou, Nikolaos E.

doi:10.1371/journal.pone.0034263

Cited by 29 publications

(25 citation statements)

References 54 publications

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“…Advances in gene sequencing techniques also continued to provide insight into new classes of cGSTs in bacteria with novel functions. Currently, seven different classes were already identified in bacteria, with some of them playing a valuable role in the biodegradation of several classes of pollutants [5,[7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Cytosolic Glutathione S-transferase in Bacteria: A Review

Shehu¹,

Abdullahi²,

Alias³

2018

Pol. J. Environ. Stud.

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Cytosolic glutathione S-transferase in bacteria possesses the biochemical capacity to degrade various classes of organochlorine pollutants in the environment in addition to their primary role of defending the organism from a wide range of endobiotics and xenobiotic substrates. Furthermore, the ability of different classes of cGST to recognize a wide repertoire of substrates due the variability in the substrate binding site of the enzymes makes them well suited for bioremediation purposes. cGSTs act as dehalogenases promoting a rapid degradation of various organochlorine compounds. Dehalogenation served as the primary mechanism for detoxification of various organochlorine compounds, making them vulnerable to attack by other degradative enzymes. However, despite their potential and advantage of wide substrate specificity, cGSTs have not been exploited for bioremediation purposes. In this review, we described the various cGST classes in bacteria and their phylogenetic relationships. Furthermore, the review reiterated that cGSTs in bacteria are involved in dehalogenation reaction, and this property can be harnessed for bioremediation of a diverse class of organochlorine pollutants as they currently represent the largest class of pollutants in the environment.

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Section: Introductionmentioning

confidence: 99%

Cytosolic Glutathione S-transferase in Bacteria: A Review

Shehu¹,

Abdullahi²,

Alias³

2018

Pol. J. Environ. Stud.

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“…However, there is a great diversity in this enzyme, with various functions still unknown [21], [63]–[64].…”

Section: Resultsmentioning

confidence: 99%

Mechanisms of Tolerance and High Degradation Capacity of the Herbicide Mesotrione by Escherichia coli Strain DH5-α

et al. 2014

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The intensive use of agrochemicals has played an important role in increasing agricultural production. One of the impacts of agrochemical use has been changes in population structure of soil microbiota. The aim of this work was to analyze the adaptive strategies that bacteria use to overcome oxidative stress caused by mesotrione, which inhibits 4-hydroxyphenylpyruvate dioxygenase. We also examined antioxidative stress systems, saturation changes of lipid membranes, and the capacity of bacteria to degrade mesotrione. Escherichia coli DH5-á was chosen as a non-environmental strain, which is already a model bacterium for studying metabolism and adaptation. The results showed that this bacterium was able to tolerate high doses of the herbicide (10× field rate), and completely degraded mesotrione after 3 h of exposure, as determined by a High Performance Liquid Chromatography. Growth rates in the presence of mesotrione were lower than in the control, prior to the period of degradation, showing toxic effects of this herbicide on bacterial cells. Changes in the saturation of the membrane lipids reduced the damage caused by reactive oxygen species and possibly hindered the entry of xenobiotics in the cell, while activating glutathione-S-transferase enzyme in the antioxidant system and in the metabolizing process of the herbicide. Considering that E. coli DH5-α is a non-environmental strain and it had no previous contact with mesotrione, the defense system found in this strain could be considered non-specific. This bacterium system response may be a general adaptation mechanism by which bacterial strains resist to damage from the presence of herbicides in agricultural soils.

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“…Labrou's group [88] have recently reported a GST from A. tumefaciens which represents a novel class of bacterial GST superfamily. Its active site is quite different from cytosolic GST reported so far.…”

Section: Catalytic Promiscuity: Beyond Lipasesmentioning

confidence: 99%

Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

Arora

Mukherjee

Gupta

2014

Sustain Chem Process

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Enzyme promiscuity can be classified into substrate promiscuity, condition promiscuity and catalytic promiscuity. Enzyme promiscuity results in far larger ranges of organic compounds which can be obtained by biocatalysis. While early examples mostly involved use of lipases, more recent literature shows that catalytic promiscuity occurs more widely and many other classes of enzymes can be used to obtain diverse kinds of molecules. This is of immense relevance in the context of white biotechnology as enzyme catalysed reactions use greener conditions.

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A Glutathione Transferase from Agrobacterium tumefaciens Reveals a Novel Class of Bacterial GST Superfamily

Cited by 29 publications

References 54 publications

Cytosolic Glutathione S-transferase in Bacteria: A Review

Cytosolic Glutathione S-transferase in Bacteria: A Review

Mechanisms of Tolerance and High Degradation Capacity of the Herbicide Mesotrione by Escherichia coli Strain DH5-α

Enzyme promiscuity: using the dark side of enzyme specificity in white biotechnology

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