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W126A - site-directed mutagenesis, H-site mutation, the mutant shows increased activity compared to the wild-type enzyme W234K - site-directed mutagenesis, isozyme GST T1-1, the mutant shows altered substrate specificity compared to the wild-type enzyme Y108A - mutant enzyme shows 58% of the wild-type activity with 1,2-dichloro-4-nitrobenzene as substrate and 37% of the wild-type activity with 1,2-epoxy-3-(p-nitrophenoxy)propane, 2% of the wild-type GSH peroxidase activity towards cumene hydroperoxide and 163% of the wild-type steroid isomerase activity towards DELTA5-androstene-3,17-dione Y108F - mutant enzyme is as active as wild-type enzyme with 1,2-dichloro-4-nitrobenzene as substrate and shows 7% of the wild-type activity with 1,2-epoxy-3-(p-nitrophenoxy)propane, 77% of the wild-type GSH peroxidase activity towards cumene hydroperoxide and 149% of the wild-type steroid isomerase activity towards DELTA5-androstene-3,17-dione
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10.1016/j.freeradbiomed.2017.01.033 [DOI] [PubMed] [Google Scholar] Chen X, Shi C, He M, Xiong S, Xia X (2023a) Endoplasmic reticulum stress: molecular mechanism and therapeutic targets
