کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5512354 | 1540224 | 2017 | 27 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization and functional analysis of a recombinant tau class glutathione transferase GmGSTU2-2 from Glycine max
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کلمات کلیدی
CuOOHDTTGSHGSTSSEDHARdehydroascorbate reductaseCDNBGSTTH-site1-chloro-2,4-dinitrobenzene - 1-کلرو-2،4-دینیتروبنزنt-BuOOH - T-BuOOHBiotic and abiotic stress - استرس زیستی و بی روحیtert-butyl peroxide - تربت بوتیل پراکسیدG-site - سایت GHerbicide detoxification - سم زدایی علف کشSecondary structure elements - عناصر ساختاری ثانویهMolecular modeling - مدل سازی مولکولیcumene hydroperoxide - هیدروپراکسید کومنEnzyme catalysis - کاتالیزور آنزیمGlutathione - گلوتاتیونGlutathione transferase - گلوتاتیون ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The plant tau class glutathione transferases (GSTs) perform diverse catalytic as well as non-catalytic roles in detoxification of xenobiotics, prevention of oxidative damage and endogenous metabolism. In the present work, the tau class isoenzyme GSTU2-2 from Glycine max (GmGSTU2-2) was characterized. Gene expression analysis of GmGSTU2 suggested a highly specific and selective induction pattern to osmotic stresses, indicating that gene expression is controlled by a specific mechanism. Purified, recombinant GmGSTU2-2 was shown to exhibit wide-range specificity towards xenobiotic compounds and ligand-binding properties, suggesting that the isoenzyme could provide catalytic flexibility in numerous metabolic conditions. Homology modeling and phylogenetic analysis suggested that the catalytic and ligand binding sites of GmGSTU2-2 are well conserved compared to other tau class GSTs. Structural analysis identified key amino acid residues in the hydrophobic binding site and provided insights into the substrate specificity of this enzyme. The results established that GmGSTU2-2 participates in a broad network of catalytic and regulatory functions involved in the plant stress response.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 94, Part B, January 2017, Pages 802-812
Journal: International Journal of Biological Macromolecules - Volume 94, Part B, January 2017, Pages 802-812
نویسندگان
Katholiki Skopelitou, Abdi W. Muleta, Anastassios C. Papageorgiou, Evangelia G. Chronopoulou, Ourania Pavli, Emmanouil Flemetakis, Georgios N. Skaracis, Nikolaos E. Labrou,