A1 Refereed original research article in a scientific journal
Structural and Functional Characterization of Camelus dromedarius Glutathione Transferase M1-1
Authors: Perperopoulou Fereniki, Poudel Nirmal, Papageorgiou Anastassios C, Ataya Farid S, Labrou Nikolaos E.
Publisher: MDPI
Publishing place: Basel
Publication year: 2022
Journal: Life
Journal name in source: LIFE-BASEL
Journal acronym: LIFE-BASEL
Article number: 106
Volume: 12
Issue: 1
Number of pages: 15
eISSN: 2075-1729
DOI: https://doi.org/10.3390/life12010106
Web address : https://doi.org/10.3390/life12010106
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/174867634
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 CdGS tau M1-1 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 CdGS tau M1-1 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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