Interaction of organotin compounds with three major glutathione S-transferases in zebrafish

Mihaljević, Ivan; Bašica, Branka; Maraković, Nikola; Kovačević, Radmila; Smital, Tvrtko

doi:10.1016/j.tiv.2019.104713

Cited by 7 publications

(3 citation statements)

References 45 publications

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“…In addition to GR and GPx, GST, as an enzyme mediator that binds GSH to hazardous compounds, plays a crucial role in the process of cell detoxification. As an electrophilic target, GSH can attack GSH nucleophiles by binding active sites, thus achieving antioxidant and detoxification functions (Mihaljevic et al, 2020). Figure 11 shows that GST activity in all fish lymphocytes exposed to ANTX-a in vitro for 12 h decreased in a dose-dependent manner regardless of treatment concentration.…”

Section: Discussionmentioning

confidence: 99%

Neurotoxic Anatoxin-a Can Also Exert Immunotoxicity by the Induction of Apoptosis on Carassius auratus Lymphocytes in vitro When Exposed to Environmentally Relevant Concentrations

Zhong

Shen

et al. 2020

Front. Physiol.

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Section: Discussionmentioning

confidence: 99%

Neurotoxic Anatoxin-a Can Also Exert Immunotoxicity by the Induction of Apoptosis on Carassius auratus Lymphocytes in vitro When Exposed to Environmentally Relevant Concentrations

Zhong

Shen

et al. 2020

Front. Physiol.

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“…Glutathione transferases (GSTs; EC. 2.5.1.18) are a widely spread family of enzymes found in both eukaryotes and prokaryotes [1,2]. They catalyze the conjugation of glutathione (GSH) with a range of hydrophobic xenobiotic compounds such as drugs, environmental pollutants, and pesticides, including chloroacetanilide herbicides [3][4][5][6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

Directed Evolution of a Glutathione Transferase for the Development of a Biosensor for Alachlor Determination

et al. 2021

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In the present work, DNA recombination of three homologous tau class glutathione transferases (GSTUs) allowed the creation of a library of tau class GmGSTUs. The library was activity screened for the identification of glutathione transferase (GST) variants with enhanced catalytic activity towards the herbicide alachlor (2-chloro-2′,6′-diethyl-N-(methoxymethyl)acetanilide). One enzyme variant (GmGSTsf) with improved catalytic activity and binding affinity for alachlor was identified and explored for the development of an optical biosensor for alachlor determination. Kinetics analysis and molecular modeling studies revealed a key mutation (Ile69Val) at the subunit interface (helix α3) that appeared to be responsible for the altered catalytic properties. The enzyme was immobilized directly on polyvinylidenefluoride membrane by crosslinking with glutaraldehyde and was placed on the inner surface of a plastic cuvette. The rate of pH changes observed as a result of the enzyme reaction was followed optometrically using a pH indicator. A calibration curve indicated that the linear concentration range for alachlor was 30–300 μM. The approach used in the present study can provide tools for the generation of novel enzymes for eco-efficient and environment-friendly analytical technologies. In addition, the outcome of this study gives an example for harnessing protein symmetry for enzyme design.

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“…These factors activate a detoxification mechanism, consisting of two phases (phase I and phase II) [3]. In phase II reactions, glutathione transferases (GSTs) are involved and encoded by multiple genes [4]. Upon entering the living cell, xenobiotic and toxic compounds may undergo GST-mediated conjugation with glutathione (GSH) in order to become more soluble and to be excreted by the cell [5].…”

Section: Introductionmentioning

confidence: 99%

Structural and Functional Characterization of Camelus dromedarius Glutathione Transferase M1-1

Perperopoulou

Poudel

Papageorgiou

et al. 2022

Life

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Glutathione transferases (GSTs; EC. 2.5.1.18) are a large family of multifunctional enzymes that play crucial roles in the metabolism and inactivation of a broad range of xenobiotic compounds. In the present work, we report the kinetic and structural characterization of the isoenzyme GSTM1-1 from Camelus dromedarius (CdGSTM1-1). The CdGSΤM1-1 was expressed in E. coli BL21 (DE3) and was purified by affinity chromatography. Kinetics analysis showed that the enzyme displays a relative narrow substrate specificity and restricted ability to bind xenobiotic compounds. The crystal structures of CdGSΤM1-1 were determined by X-ray crystallography in complex with the substrate (GSH) or the reaction product (S-p-nitrobenzyl-GSH), providing snapshots of the induced-fit catalytic mechanism. The thermodynamic stability of CdGSTM1-1 was investigated using differential scanning fluorimetry (DSF) in the absence and in presence of GSH and S-p-nitrobenzyl-GSH and revealed that the enzyme’s structure is significantly stabilized by its ligands. The results of the present study advance the understanding of camelid GST detoxification mechanisms and their contribution to abiotic stress adaptation in harsh desert conditions.

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Interaction of organotin compounds with three major glutathione S-transferases in zebrafish

Cited by 7 publications

References 45 publications

Neurotoxic Anatoxin-a Can Also Exert Immunotoxicity by the Induction of Apoptosis on Carassius auratus Lymphocytes in vitro When Exposed to Environmentally Relevant Concentrations

Neurotoxic Anatoxin-a Can Also Exert Immunotoxicity by the Induction of Apoptosis on Carassius auratus Lymphocytes in vitro When Exposed to Environmentally Relevant Concentrations

Directed Evolution of a Glutathione Transferase for the Development of a Biosensor for Alachlor Determination

Structural and Functional Characterization of Camelus dromedarius Glutathione Transferase M1-1

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