Cytosolic Glutathione S-transferase in Bacteria: A Review
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Department of Biochemistry, Institute of Biological Sciences, University of Malaya, Kuala Lumpur, Malaysia
Department of Biochemistry, Bayero University, Kano, Nigeria
Submission date: 2017-10-18
Final revision date: 2017-12-03
Acceptance date: 2018-02-10
Online publication date: 2018-09-10
Publication date: 2018-12-20
Corresponding author
Dayyabu Shehu   

University of Malaya, Lab E, 1.2, Block E. Institute of Biological sciences, University of Malaya., 50603 Kuala Lumpur, Malaysia
Pol. J. Environ. Stud. 2019;28(2):515-528
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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