Directed evolution of glutathione transferases towards a selective glutathione-binding site and improved oxidative stability

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• 作者：Irine Axarli^a ; Abdi W. Muleta^b ; Evangelia G. Chronopoulou^a ; Anastassios C. Papageorgiou^b ; Nikolaos E. Labrou^a ; ^{lambrou@aua.gr}
• 关键词：CDNB ; 1-chloro-2 ; 4-dinitrobenzene ; GSH ; glutathione ; GST ; glutathione transferase ; hGSTA1-1 ; human glutathione transferase A1-1 ; rGSTA1-1 ; rat glutathione transferase A1-1 ; Sj26GST ; the GST isoenzyme from Schistosoma japonicum
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1861
• 期：1
• 页码：3416-3428
• 全文大小：1943 K
• 卷排序：1861

文摘

GSTs are enzymes involved in the metabolism of xenobiotics. A GST (GSTD4) was created through DNA shuffling and showed high affinity towards GSH. The crystal structure of the GSTD4 enzyme was determined. The GSTD4 enzyme was further optimized for improved oxidative stability. The GSTD4 enzyme could be useful as affinity and catalytic tool in biotechnology.