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hydroperoxy fatty acid:NADPH oxidorductase
The enzyme, characterized from the cyanobacterium Synechocystis PCC 6803, can reduce unsaturated fatty acid hydroperoxides and alkyl hydroperoxides. The enzyme, which utilizes NADPH generated by the photosynthetic electron transfer system, protects the cells from lipid peroxidation.
the enzyme does not use reduced glutathione as an electron donor. No activity with H2O2, phosphatidylcholine hydroperoxide and digalactosyl diacylglycerol hydroperoxide. Neither cytochrome c nor ascorbate substitute for NADPH as an electron donor
the steady-state transcript level of gpx-1 gradually increases under oxidative stress conditions imposed by high light intensity (0.35 mE m.2 s-1), high salinity (200 mM NaCl), or application of methyl viologen (0.001 mM) or tert-butyl hydroperoxide (0.001 mM) in the wild type and GPX-2 knock-out mutant cells. The protein level of GPX-2 increases approximately 3fold and 1.6fold at 3 h with the methyl viologen and NaCl treatments, respectively. Under high light conditions, the protein level of GPX-2 increases approximately 1.2fold
Gaber, A.; Yoshimura, K.; Tamoi, M.; Takeda, T.; Nakano, Y.; Shigeoka, S.
Induction and functional analysis of two reduced nicotinamide adenine dinucleotide phosphate-dependent glutathione peroxidase-like proteins in Synechocystis PCC 6803 during the progression of oxidative stress